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Iron in PDB 4qon: Structure of Bacillus Pumilus Catalase with Catechol Bound.

Enzymatic activity of Structure of Bacillus Pumilus Catalase with Catechol Bound.

All present enzymatic activity of Structure of Bacillus Pumilus Catalase with Catechol Bound.:
1.11.1.6;

Protein crystallography data

The structure of Structure of Bacillus Pumilus Catalase with Catechol Bound., PDB code: 4qon was solved by P.C.Loewen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 109.12 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 92.140, 109.116, 103.695, 90.00, 92.20, 90.00
R / Rfree (%) 20.6 / 23.8

Other elements in 4qon:

The structure of Structure of Bacillus Pumilus Catalase with Catechol Bound. also contains other interesting chemical elements:

Chlorine (Cl) 6 atoms
Sodium (Na) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Bacillus Pumilus Catalase with Catechol Bound. (pdb code 4qon). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Structure of Bacillus Pumilus Catalase with Catechol Bound., PDB code: 4qon:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 4qon

Go back to Iron Binding Sites List in 4qon
Iron binding site 1 out of 8 in the Structure of Bacillus Pumilus Catalase with Catechol Bound.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Bacillus Pumilus Catalase with Catechol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:16.0
occ:0.50
 FE A:HEM501 0.0 16.0 0.5
FE A:HEM502 0.7 21.5 0.5
NA A:HEM502 1.3 18.9 0.5
OH A:TYR340 1.9 18.8 1.0
ND A:HEM501 1.9 15.2 0.5
NA A:HEM501 2.0 14.4 0.5
NC A:HEM501 2.1 15.6 0.5
NB A:HEM502 2.1 19.2 0.5
NB A:HEM501 2.1 15.0 0.5
ND A:HEM502 2.1 17.9 0.5
C4A A:HEM502 2.4 18.3 0.5
C1A A:HEM502 2.5 17.9 0.5
NC A:HEM502 2.7 19.2 0.5
C1B A:HEM502 2.8 19.4 0.5
C1D A:HEM501 2.9 15.0 0.5
C4D A:HEM502 2.9 17.3 0.5
C4D A:HEM501 2.9 14.7 0.5
CZ A:TYR340 2.9 20.2 1.0
CHB A:HEM502 2.9 18.9 0.5
C4C A:HEM501 3.0 15.6 0.5
C1A A:HEM501 3.0 14.2 0.5
CHA A:HEM502 3.1 17.6 0.5
C4B A:HEM501 3.1 15.2 0.5
C1B A:HEM501 3.1 14.9 0.5
C1C A:HEM501 3.1 15.5 0.5
C4A A:HEM501 3.1 14.4 0.5
C4B A:HEM502 3.2 19.2 0.5
CHD A:HEM501 3.3 15.4 0.5
O3 A:CAQ503 3.3 28.5 1.0
CHA A:HEM501 3.4 14.4 0.5
C1D A:HEM502 3.4 17.6 0.5
CHC A:HEM501 3.5 15.2 0.5
CHB A:HEM501 3.5 14.3 0.5
C3A A:HEM502 3.6 17.8 0.5
C2A A:HEM502 3.6 17.7 0.5
C1C A:HEM502 3.6 19.1 0.5
CE2 A:TYR340 3.6 20.3 1.0
C4C A:HEM502 3.7 18.8 0.5
CE1 A:TYR340 3.8 19.4 1.0
CHC A:HEM502 3.9 18.8 0.5
CHD A:HEM502 4.0 17.7 0.5
C2B A:HEM502 4.1 19.2 0.5
C2D A:HEM501 4.1 14.8 0.5
C3D A:HEM501 4.1 14.6 0.5
NE A:ARG336 4.1 19.2 1.0
NH2 A:ARG336 4.1 20.9 1.0
C3C A:HEM501 4.2 15.6 0.5
C2C A:HEM501 4.2 15.6 0.5
C3D A:HEM502 4.3 16.3 0.5
C2A A:HEM501 4.3 13.6 0.5
C3B A:HEM502 4.3 19.1 0.5
C2B A:HEM501 4.3 14.9 0.5
C3A A:HEM501 4.3 13.8 0.5
C3B A:HEM501 4.3 15.0 0.5
C2D A:HEM502 4.5 16.7 0.5
NE2 A:HIS57 4.5 18.3 1.0
CZ A:ARG336 4.5 20.0 1.0
CD2 A:HIS57 4.6 17.4 1.0
C3 A:CAQ503 4.7 27.2 1.0
CG2 A:VAL56 4.7 17.1 1.0
O4 A:CAQ503 4.8 25.9 1.0
C2C A:HEM502 4.8 18.7 0.5
CZ A:PHE143 4.8 17.7 1.0
C3C A:HEM502 4.9 18.6 0.5
CD2 A:TYR340 4.9 19.9 1.0
CMA A:HEM502 5.0 17.8 0.5
CAA A:HEM502 5.0 17.6 0.5

Iron binding site 2 out of 8 in 4qon

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Iron binding site 2 out of 8 in the Structure of Bacillus Pumilus Catalase with Catechol Bound.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Bacillus Pumilus Catalase with Catechol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:21.5
occ:0.50
 FE A:HEM502 0.0 21.5 0.5
FE A:HEM501 0.7 16.0 0.5
NB A:HEM501 1.4 15.0 0.5
ND A:HEM502 1.9 17.9 0.5
NA A:HEM501 2.0 14.4 0.5
NA A:HEM502 2.0 18.9 0.5
NC A:HEM502 2.0 19.2 0.5
OH A:TYR340 2.1 18.8 1.0
NB A:HEM502 2.1 19.2 0.5
NC A:HEM501 2.3 15.6 0.5
C1B A:HEM501 2.4 14.9 0.5
C4B A:HEM501 2.5 15.2 0.5
ND A:HEM501 2.6 15.2 0.5
C4A A:HEM501 2.8 14.4 0.5
C4D A:HEM502 2.9 17.3 0.5
C1D A:HEM502 2.9 17.6 0.5
CHB A:HEM501 3.0 14.3 0.5
C4C A:HEM502 3.0 18.8 0.5
CZ A:TYR340 3.0 20.2 1.0
C1C A:HEM502 3.0 19.1 0.5
C4B A:HEM502 3.0 19.2 0.5
C1A A:HEM502 3.0 17.9 0.5
C1C A:HEM501 3.0 15.5 0.5
C1B A:HEM502 3.1 19.4 0.5
C4A A:HEM502 3.1 18.3 0.5
CHC A:HEM501 3.2 15.2 0.5
C1A A:HEM501 3.2 14.2 0.5
O3 A:CAQ503 3.3 28.5 1.0
CHD A:HEM502 3.4 17.7 0.5
CHA A:HEM502 3.4 17.6 0.5
C4C A:HEM501 3.4 15.6 0.5
CHC A:HEM502 3.4 18.8 0.5
C4D A:HEM501 3.5 14.7 0.5
CHB A:HEM502 3.5 18.9 0.5
C1D A:HEM501 3.6 15.0 0.5
C2B A:HEM501 3.6 14.9 0.5
C3B A:HEM501 3.7 15.0 0.5
CE1 A:TYR340 3.7 19.4 1.0
CHA A:HEM501 3.8 14.4 0.5
CE2 A:TYR340 3.9 20.3 1.0
CHD A:HEM501 3.9 15.4 0.5
NE A:ARG336 4.0 19.2 1.0
C3A A:HEM501 4.1 13.8 0.5
C3C A:HEM502 4.2 18.6 0.5
C2C A:HEM502 4.2 18.7 0.5
C3D A:HEM502 4.2 16.3 0.5
C2D A:HEM502 4.2 16.7 0.5
C2A A:HEM502 4.2 17.7 0.5
C3A A:HEM502 4.3 17.8 0.5
C2B A:HEM502 4.3 19.2 0.5
CZ A:PHE143 4.3 17.7 1.0
C3B A:HEM502 4.3 19.1 0.5
C2A A:HEM501 4.3 13.6 0.5
C2C A:HEM501 4.3 15.6 0.5
NH2 A:ARG336 4.4 20.9 1.0
C3C A:HEM501 4.5 15.6 0.5
C3 A:CAQ503 4.6 27.2 1.0
CG2 A:VAL56 4.7 17.1 1.0
CZ A:ARG336 4.7 20.0 1.0
C3D A:HEM501 4.8 14.6 0.5
CE1 A:PHE143 4.8 18.7 1.0
C2D A:HEM501 4.8 14.8 0.5
CE2 A:PHE143 4.9 17.9 1.0
CD1 A:TYR340 4.9 18.7 1.0
CD A:ARG336 4.9 18.3 1.0
NE2 A:HIS57 5.0 18.3 1.0
CD2 A:HIS57 5.0 17.4 1.0

Iron binding site 3 out of 8 in 4qon

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Iron binding site 3 out of 8 in the Structure of Bacillus Pumilus Catalase with Catechol Bound.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Bacillus Pumilus Catalase with Catechol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:16.8
occ:0.50
 FE B:HEM501 0.0 16.8 0.5
FE B:HEM502 0.6 11.8 0.5
NB B:HEM502 1.7 11.2 0.5
ND B:HEM501 1.9 13.9 0.5
NC B:HEM502 1.9 11.0 0.5
NA B:HEM501 2.0 14.0 0.5
NB B:HEM501 2.1 14.3 0.5
NC B:HEM501 2.1 14.2 0.5
OH B:TYR340 2.2 13.8 1.0
NA B:HEM502 2.2 10.9 0.5
ND B:HEM502 2.4 10.6 0.5
C4B B:HEM502 2.6 11.1 0.5
C1C B:HEM502 2.7 11.1 0.5
C1B B:HEM502 2.8 11.2 0.5
C4D B:HEM501 2.9 13.7 0.5
C1D B:HEM501 2.9 13.8 0.5
O3 B:CAQ503 3.0 27.5 1.0
C4C B:HEM501 3.0 14.2 0.5
C4B B:HEM501 3.0 14.1 0.5
C1B B:HEM501 3.0 14.0 0.5
CHC B:HEM502 3.0 11.0 0.5
C1A B:HEM501 3.1 13.4 0.5
C4C B:HEM502 3.1 10.9 0.5
C4A B:HEM502 3.1 10.9 0.5
C4A B:HEM501 3.1 13.8 0.5
C1C B:HEM501 3.1 14.3 0.5
CZ B:TYR340 3.3 13.7 1.0
CHB B:HEM502 3.3 11.0 0.5
C1A B:HEM502 3.3 10.7 0.5
C1D B:HEM502 3.3 10.5 0.5
CHD B:HEM501 3.4 13.7 0.5
C4D B:HEM502 3.4 10.4 0.5
CHA B:HEM501 3.4 13.6 0.5
CHC B:HEM501 3.5 14.4 0.5
CHB B:HEM501 3.5 14.0 0.5
CHD B:HEM502 3.6 10.6 0.5
CHA B:HEM502 3.8 10.5 0.5
C3B B:HEM502 3.9 11.3 0.5
C2B B:HEM502 3.9 11.1 0.5
C2C B:HEM502 4.0 11.1 0.5
CE1 B:TYR340 4.0 13.6 1.0
CE2 B:TYR340 4.1 13.5 1.0
NE B:ARG336 4.1 13.9 1.0
C3C B:HEM502 4.1 10.9 0.5
C2D B:HEM501 4.1 13.5 0.5
C3D B:HEM501 4.2 13.6 0.5
C3C B:HEM501 4.2 13.9 0.5
C2C B:HEM501 4.2 14.5 0.5
C3B B:HEM501 4.2 14.0 0.5
C2B B:HEM501 4.2 13.7 0.5
C3 B:CAQ503 4.3 24.2 1.0
C2A B:HEM501 4.3 13.1 0.5
C3A B:HEM502 4.3 10.7 0.5
C3A B:HEM501 4.3 13.4 0.5
CZ B:PHE143 4.3 14.2 1.0
NH2 B:ARG336 4.3 14.1 1.0
O4 B:CAQ503 4.3 20.9 1.0
C2A B:HEM502 4.4 10.7 0.5
NE2 B:HIS57 4.6 13.5 1.0
CZ B:ARG336 4.6 14.1 1.0
C2D B:HEM502 4.6 10.3 0.5
C3D B:HEM502 4.7 10.1 0.5
CG2 B:VAL56 4.7 11.6 1.0
CD2 B:HIS57 4.7 13.5 1.0
CE1 B:PHE143 4.8 14.5 1.0
C4 B:CAQ503 4.9 21.7 1.0

Iron binding site 4 out of 8 in 4qon

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Iron binding site 4 out of 8 in the Structure of Bacillus Pumilus Catalase with Catechol Bound.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Bacillus Pumilus Catalase with Catechol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:11.8
occ:0.50
 FE B:HEM502 0.0 11.8 0.5
FE B:HEM501 0.6 16.8 0.5
NA B:HEM501 1.6 14.0 0.5
ND B:HEM501 1.8 13.9 0.5
OH B:TYR340 1.8 13.8 1.0
ND B:HEM502 1.9 10.6 0.5
NA B:HEM502 2.0 10.9 0.5
NC B:HEM502 2.0 11.0 0.5
NB B:HEM502 2.1 11.2 0.5
NB B:HEM501 2.3 14.3 0.5
NC B:HEM501 2.6 14.2 0.5
C4D B:HEM501 2.6 13.7 0.5
C1A B:HEM501 2.6 13.4 0.5
CZ B:TYR340 2.8 13.7 1.0
C4A B:HEM501 2.8 13.8 0.5
C1D B:HEM501 2.9 13.8 0.5
C1D B:HEM502 2.9 10.5 0.5
C4D B:HEM502 2.9 10.4 0.5
C1A B:HEM502 3.0 10.7 0.5
C4A B:HEM502 3.0 10.9 0.5
C4C B:HEM502 3.0 10.9 0.5
CHA B:HEM501 3.0 13.6 0.5
C1C B:HEM502 3.0 11.1 0.5
C4B B:HEM502 3.1 11.1 0.5
C1B B:HEM502 3.1 11.2 0.5
C1B B:HEM501 3.1 14.0 0.5
CHB B:HEM501 3.3 14.0 0.5
C4C B:HEM501 3.3 14.2 0.5
C4B B:HEM501 3.4 14.1 0.5
CHD B:HEM502 3.4 10.6 0.5
CHA B:HEM502 3.4 10.5 0.5
O3 B:CAQ503 3.4 27.5 1.0
CHB B:HEM502 3.4 11.0 0.5
CHC B:HEM502 3.5 11.0 0.5
CE2 B:TYR340 3.5 13.5 1.0
CHD B:HEM501 3.5 13.7 0.5
C1C B:HEM501 3.6 14.3 0.5
CE1 B:TYR340 3.6 13.6 1.0
C2A B:HEM501 3.8 13.1 0.5
C3A B:HEM501 3.9 13.4 0.5
C3D B:HEM501 3.9 13.6 0.5
CHC B:HEM501 3.9 14.4 0.5
C2D B:HEM501 4.0 13.5 0.5
NE B:ARG336 4.1 13.9 1.0
C3A B:HEM502 4.1 10.7 0.5
C2A B:HEM502 4.2 10.7 0.5
C3C B:HEM502 4.2 10.9 0.5
C2C B:HEM502 4.2 11.1 0.5
C2D B:HEM502 4.2 10.3 0.5
C3D B:HEM502 4.2 10.1 0.5
NH2 B:ARG336 4.2 14.1 1.0
C2B B:HEM502 4.3 11.1 0.5
C3B B:HEM502 4.3 11.3 0.5
C2B B:HEM501 4.4 13.7 0.5
C3B B:HEM501 4.5 14.0 0.5
C3C B:HEM501 4.5 13.9 0.5
CZ B:ARG336 4.6 14.1 1.0
CZ B:PHE143 4.6 14.2 1.0
C2C B:HEM501 4.6 14.5 0.5
CG2 B:VAL56 4.7 11.6 1.0
CD2 B:TYR340 4.7 13.8 1.0
C3 B:CAQ503 4.8 24.2 1.0
NE2 B:HIS57 4.8 13.5 1.0
O4 B:CAQ503 4.8 20.9 1.0
CD2 B:HIS57 4.8 13.5 1.0
CD1 B:TYR340 4.8 14.1 1.0

Iron binding site 5 out of 8 in 4qon

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Iron binding site 5 out of 8 in the Structure of Bacillus Pumilus Catalase with Catechol Bound.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Structure of Bacillus Pumilus Catalase with Catechol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:13.8
occ:0.50
 FE C:HEM501 0.0 13.8 0.5
FE C:HEM502 0.6 11.5 0.5
ND C:HEM502 1.6 10.9 0.5
NA C:HEM502 1.7 10.8 0.5
ND C:HEM501 1.9 12.3 0.5
NA C:HEM501 2.0 12.0 0.5
OH C:TYR340 2.0 11.6 1.0
NC C:HEM501 2.1 12.8 0.5
NB C:HEM501 2.1 12.4 0.5
NB C:HEM502 2.5 11.3 0.5
NC C:HEM502 2.5 11.2 0.5
C1A C:HEM502 2.5 10.8 0.5
C4D C:HEM502 2.5 10.7 0.5
C1D C:HEM502 2.8 10.8 0.5
CHA C:HEM502 2.9 10.7 0.5
C4D C:HEM501 2.9 12.0 0.5
C4A C:HEM502 2.9 10.8 0.5
C1D C:HEM501 3.0 12.1 0.5
C1A C:HEM501 3.0 11.9 0.5
C4A C:HEM501 3.0 11.9 0.5
CZ C:TYR340 3.0 12.4 1.0
C4B C:HEM501 3.0 12.4 0.5
C4C C:HEM501 3.1 12.7 0.5
C1C C:HEM501 3.1 12.6 0.5
C1B C:HEM501 3.1 12.5 0.5
O4 C:CAQ504 3.2 29.6 1.0
C1B C:HEM502 3.3 11.2 0.5
C4C C:HEM502 3.3 11.2 0.5
CHA C:HEM501 3.3 11.9 0.5
CHC C:HEM501 3.5 12.5 0.5
CHD C:HEM501 3.5 12.4 0.5
CHB C:HEM501 3.5 12.1 0.5
CHB C:HEM502 3.5 10.9 0.5
CHD C:HEM502 3.5 11.0 0.5
C4B C:HEM502 3.6 11.2 0.5
C1C C:HEM502 3.6 11.2 0.5
CE2 C:TYR340 3.7 12.0 1.0
C2A C:HEM502 3.8 10.7 0.5
CE1 C:TYR340 3.9 11.8 1.0
C3D C:HEM502 3.9 10.7 0.5
C3A C:HEM502 3.9 10.6 0.5
C2D C:HEM502 4.0 10.7 0.5
CHC C:HEM502 4.0 11.3 0.5
C3D C:HEM501 4.1 11.8 0.5
C2D C:HEM501 4.2 11.8 0.5
C2A C:HEM501 4.2 11.7 0.5
C3A C:HEM501 4.2 11.8 0.5
C3C C:HEM501 4.2 12.4 0.5
C2C C:HEM501 4.3 12.5 0.5
C3B C:HEM501 4.3 12.3 0.5
C2B C:HEM501 4.4 12.3 0.5
NE C:ARG336 4.4 13.7 1.0
NH2 C:ARG336 4.4 14.2 1.0
CG2 C:VAL56 4.4 12.6 1.0
C2B C:HEM502 4.5 11.2 0.5
CD2 C:HIS57 4.5 11.6 1.0
C3C C:HEM502 4.6 11.2 0.5
NE2 C:HIS57 4.6 12.1 1.0
C4 C:CAQ504 4.6 25.2 1.0
CZ C:PHE143 4.6 13.4 1.0
C3B C:HEM502 4.7 11.3 0.5
C2C C:HEM502 4.7 11.2 0.5
O3 C:CAQ504 4.8 21.3 1.0
CZ C:ARG336 4.8 13.8 1.0
CD2 C:TYR340 4.9 11.9 1.0

Iron binding site 6 out of 8 in 4qon

Go back to Iron Binding Sites List in 4qon
Iron binding site 6 out of 8 in the Structure of Bacillus Pumilus Catalase with Catechol Bound.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Structure of Bacillus Pumilus Catalase with Catechol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe502

b:11.5
occ:0.50
 FE C:HEM502 0.0 11.5 0.5
FE C:HEM501 0.6 13.8 0.5
NB C:HEM501 1.7 12.4 0.5
NC C:HEM501 1.8 12.8 0.5
OH C:TYR340 1.9 11.6 1.0
ND C:HEM502 2.0 10.9 0.5
NA C:HEM502 2.0 10.8 0.5
NC C:HEM502 2.1 11.2 0.5
NB C:HEM502 2.1 11.3 0.5
ND C:HEM501 2.3 12.3 0.5
NA C:HEM501 2.4 12.0 0.5
C4B C:HEM501 2.5 12.4 0.5
C1C C:HEM501 2.6 12.6 0.5
C4C C:HEM501 2.9 12.7 0.5
CHC C:HEM501 2.9 12.5 0.5
C1B C:HEM501 2.9 12.5 0.5
C4D C:HEM502 3.0 10.7 0.5
CZ C:TYR340 3.0 12.4 1.0
C1D C:HEM502 3.0 10.8 0.5
C1A C:HEM502 3.0 10.8 0.5
C1B C:HEM502 3.0 11.2 0.5
C4B C:HEM502 3.0 11.2 0.5
C4C C:HEM502 3.0 11.2 0.5
C1C C:HEM502 3.1 11.2 0.5
C4A C:HEM502 3.1 10.8 0.5
C1D C:HEM501 3.2 12.1 0.5
C4A C:HEM501 3.2 11.9 0.5
O4 C:CAQ504 3.3 29.6 1.0
C4D C:HEM501 3.4 12.0 0.5
CHA C:HEM502 3.4 10.7 0.5
CHD C:HEM502 3.5 11.0 0.5
CHC C:HEM502 3.5 11.3 0.5
CHB C:HEM502 3.5 10.9 0.5
CHB C:HEM501 3.5 12.1 0.5
C1A C:HEM501 3.5 11.9 0.5
CHD C:HEM501 3.5 12.4 0.5
CE1 C:TYR340 3.7 11.8 1.0
C2C C:HEM501 3.8 12.5 0.5
CE2 C:TYR340 3.8 12.0 1.0
C3B C:HEM501 3.9 12.3 0.5
NE C:ARG336 3.9 13.7 1.0
CHA C:HEM501 3.9 11.9 0.5
C3C C:HEM501 3.9 12.4 0.5
C2B C:HEM501 4.0 12.3 0.5
NH2 C:ARG336 4.1 14.2 1.0
C2B C:HEM502 4.2 11.2 0.5
C3C C:HEM502 4.2 11.2 0.5
C2A C:HEM502 4.2 10.7 0.5
C3B C:HEM502 4.2 11.3 0.5
C2C C:HEM502 4.2 11.2 0.5
C3A C:HEM502 4.2 10.6 0.5
C2D C:HEM502 4.3 10.7 0.5
C3D C:HEM502 4.3 10.7 0.5
CZ C:ARG336 4.4 13.8 1.0
C3A C:HEM501 4.5 11.8 0.5
CZ C:PHE143 4.5 13.4 1.0
C2D C:HEM501 4.5 11.8 0.5
C4 C:CAQ504 4.6 25.2 1.0
C3D C:HEM501 4.6 11.8 0.5
C2A C:HEM501 4.6 11.7 0.5
O3 C:CAQ504 4.8 21.3 1.0
CD C:ARG336 4.8 13.5 1.0
CG2 C:VAL56 4.8 12.6 1.0
NE2 C:HIS57 4.9 12.1 1.0
CE1 C:PHE143 4.9 14.1 1.0
CD2 C:HIS57 5.0 11.6 1.0
CD1 C:TYR340 5.0 11.8 1.0

Iron binding site 7 out of 8 in 4qon

Go back to Iron Binding Sites List in 4qon
Iron binding site 7 out of 8 in the Structure of Bacillus Pumilus Catalase with Catechol Bound.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Structure of Bacillus Pumilus Catalase with Catechol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:23.7
occ:0.50
 FE D:HEM501 0.0 23.7 0.5
FE D:HEM502 0.4 13.2 0.5
ND D:HEM502 1.7 12.5 0.5
NA D:HEM502 1.9 13.0 0.5
ND D:HEM501 1.9 20.2 0.5
NA D:HEM501 2.0 19.2 0.5
NB D:HEM501 2.1 20.1 0.5
NC D:HEM501 2.1 20.7 0.5
OH D:TYR340 2.1 16.0 1.0
NC D:HEM502 2.3 12.6 0.5
NB D:HEM502 2.4 13.1 0.5
C4D D:HEM502 2.7 12.2 0.5
C1A D:HEM502 2.8 12.4 0.5
C1D D:HEM502 2.8 12.1 0.5
O4 D:CAQ503 2.9 27.0 1.0
C4D D:HEM501 2.9 19.1 0.5
C1D D:HEM501 2.9 19.5 0.5
C1A D:HEM501 3.0 18.5 0.5
C4A D:HEM501 3.0 18.3 0.5
C4A D:HEM502 3.0 12.7 0.5
C1B D:HEM501 3.1 18.8 0.5
C4B D:HEM501 3.1 19.8 0.5
CZ D:TYR340 3.1 16.2 1.0
C4C D:HEM501 3.1 20.4 0.5
CHA D:HEM502 3.1 12.4 0.5
C1C D:HEM501 3.1 20.3 0.5
C4C D:HEM502 3.2 12.1 0.5
C1B D:HEM502 3.3 12.9 0.5
C4B D:HEM502 3.4 12.8 0.5
CHA D:HEM501 3.4 18.8 0.5
CHD D:HEM502 3.4 11.8 0.5
C1C D:HEM502 3.4 12.4 0.5
CHD D:HEM501 3.4 19.8 0.5
CHB D:HEM501 3.5 17.7 0.5
CHC D:HEM501 3.5 20.3 0.5
CHB D:HEM502 3.6 12.9 0.5
CE2 D:TYR340 3.7 16.3 1.0
CHC D:HEM502 3.8 12.7 0.5
CE1 D:TYR340 3.9 16.8 1.0
C3D D:HEM502 4.0 12.0 0.5
C2D D:HEM502 4.0 11.9 0.5
C2A D:HEM502 4.0 12.6 0.5
C3D D:HEM501 4.1 19.3 0.5
C3A D:HEM502 4.1 12.5 0.5
C2D D:HEM501 4.2 19.2 0.5
C2A D:HEM501 4.2 17.7 0.5
C3A D:HEM501 4.2 17.7 0.5
C4 D:CAQ503 4.3 27.5 1.0
C2B D:HEM501 4.3 17.9 0.5
C3C D:HEM501 4.3 20.3 0.5
C3B D:HEM501 4.3 18.8 0.5
C2C D:HEM501 4.3 20.3 0.5
NE D:ARG336 4.3 21.6 1.0
CG2 D:VAL56 4.4 15.1 1.0
NH2 D:ARG336 4.4 21.2 1.0
C3C D:HEM502 4.4 11.8 0.5
CD2 D:HIS57 4.5 16.2 1.0
C2B D:HEM502 4.5 12.9 0.5
NE2 D:HIS57 4.5 18.0 1.0
C2C D:HEM502 4.5 12.1 0.5
CZ D:PHE143 4.6 17.2 1.0
C3B D:HEM502 4.6 12.9 0.5
O3 D:CAQ503 4.6 24.9 1.0
CZ D:ARG336 4.8 21.8 1.0
CD2 D:TYR340 5.0 15.8 1.0

Iron binding site 8 out of 8 in 4qon

Go back to Iron Binding Sites List in 4qon
Iron binding site 8 out of 8 in the Structure of Bacillus Pumilus Catalase with Catechol Bound.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Structure of Bacillus Pumilus Catalase with Catechol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe502

b:13.2
occ:0.50
 FE D:HEM502 0.0 13.2 0.5
FE D:HEM501 0.4 23.7 0.5
OH D:TYR340 1.9 16.0 1.0
NC D:HEM501 1.9 20.7 0.5
NB D:HEM501 1.9 20.1 0.5
ND D:HEM502 1.9 12.5 0.5
NA D:HEM502 2.0 13.0 0.5
NB D:HEM502 2.1 13.1 0.5
NC D:HEM502 2.1 12.6 0.5
ND D:HEM501 2.1 20.2 0.5
NA D:HEM501 2.3 19.2 0.5
C4B D:HEM501 2.8 19.8 0.5
C1C D:HEM501 2.8 20.3 0.5
C4C D:HEM501 2.9 20.4 0.5
CZ D:TYR340 2.9 16.2 1.0
C1D D:HEM502 3.0 12.1 0.5
C1B D:HEM501 3.0 18.8 0.5
C4D D:HEM502 3.0 12.2 0.5
C1D D:HEM501 3.0 19.5 0.5
C1A D:HEM502 3.0 12.4 0.5
O4 D:CAQ503 3.0 27.0 1.0
C4B D:HEM502 3.0 12.8 0.5
C1B D:HEM502 3.1 12.9 0.5
C4C D:HEM502 3.1 12.1 0.5
C4A D:HEM502 3.1 12.7 0.5
C1C D:HEM502 3.1 12.4 0.5
C4D D:HEM501 3.2 19.1 0.5
C4A D:HEM501 3.2 18.3 0.5
CHC D:HEM501 3.2 20.3 0.5
C1A D:HEM501 3.3 18.5 0.5
CHD D:HEM501 3.4 19.8 0.5
CHA D:HEM502 3.4 12.4 0.5
CHD D:HEM502 3.4 11.8 0.5
CHB D:HEM502 3.5 12.9 0.5
CHC D:HEM502 3.5 12.7 0.5
CHB D:HEM501 3.5 17.7 0.5
CHA D:HEM501 3.7 18.8 0.5
CE2 D:TYR340 3.7 16.3 1.0
CE1 D:TYR340 3.7 16.8 1.0
NE D:ARG336 3.9 21.6 1.0
C2C D:HEM501 4.0 20.3 0.5
C3C D:HEM501 4.0 20.3 0.5
C3B D:HEM501 4.1 18.8 0.5
C2B D:HEM501 4.1 17.9 0.5
NH2 D:ARG336 4.1 21.2 1.0
C2D D:HEM502 4.2 11.9 0.5
C2A D:HEM502 4.3 12.6 0.5
C3A D:HEM502 4.3 12.5 0.5
C3C D:HEM502 4.3 11.8 0.5
C2B D:HEM502 4.3 12.9 0.5
C3B D:HEM502 4.3 12.9 0.5
C3D D:HEM502 4.3 12.0 0.5
C2C D:HEM502 4.3 12.1 0.5
C2D D:HEM501 4.3 19.2 0.5
C3D D:HEM501 4.4 19.3 0.5
C4 D:CAQ503 4.4 27.5 1.0
CZ D:ARG336 4.4 21.8 1.0
C3A D:HEM501 4.5 17.7 0.5
C2A D:HEM501 4.5 17.7 0.5
CZ D:PHE143 4.7 17.2 1.0
O3 D:CAQ503 4.7 24.9 1.0
CG2 D:VAL56 4.8 15.1 1.0
NE2 D:HIS57 4.8 18.0 1.0
CD2 D:HIS57 4.8 16.2 1.0
CD D:ARG336 4.9 19.9 1.0
CD1 D:TYR340 5.0 16.0 1.0
CD2 D:TYR340 5.0 15.8 1.0

Reference:

P.C.Loewen, J.Villanueva, J.Switala, L.J.Donald, A.Ivancich. Unprecedented Access of Phenolic Substrates to the Heme Active Site of A Catalase: Substrate Binding and Peroxidase-Like Reactivity of Bacillus Pumilus Catalase Monitored By X-Ray Crystallography and Epr Spectroscopy. Proteins 2015.
ISSN: ESSN 1097-0134
PubMed: 25663126
DOI: 10.1002/PROT.24777
Page generated: Sun Dec 13 15:44:59 2020

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