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Iron in PDB 4qor: Structure of Bacillus Pumilus Catalase with Chlorophenol Bound.

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

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

Protein crystallography data

The structure of Structure of Bacillus Pumilus Catalase with Chlorophenol Bound., PDB code: 4qor 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) 102.97 / 1.95
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 91.660, 109.080, 103.030, 90.00, 91.90, 90.00
R / Rfree (%) 18.2 / 22

Other elements in 4qor:

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

Chlorine (Cl) 12 atoms
Sodium (Na) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Bacillus Pumilus Catalase with Chlorophenol Bound. (pdb code 4qor). 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 Chlorophenol Bound., PDB code: 4qor:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 4qor

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Iron binding site 1 out of 8 in the Structure of Bacillus Pumilus Catalase with Chlorophenol 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 Chlorophenol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:20.6
occ:0.50
 FE A:HEM501 0.0 20.6 0.5
FE A:HEM502 0.7 15.4 0.5
NA A:HEM502 1.4 14.7 0.5
ND A:HEM501 1.9 18.2 0.5
NA A:HEM501 2.0 18.2 0.5
OH A:TYR340 2.0 18.9 1.0
NC A:HEM501 2.1 18.8 0.5
ND A:HEM502 2.1 14.3 0.5
NB A:HEM502 2.1 14.8 0.5
NB A:HEM501 2.1 19.2 0.5
C4A A:HEM502 2.4 14.8 0.5
C1A A:HEM502 2.5 14.5 0.5
NC A:HEM502 2.7 14.5 0.5
C1B A:HEM502 2.8 15.1 0.5
C4D A:HEM502 2.8 14.4 0.5
C1D A:HEM501 2.9 18.5 0.5
C4D A:HEM501 2.9 18.1 0.5
CHB A:HEM502 3.0 14.8 0.5
C4C A:HEM501 3.0 19.0 0.5
CHA A:HEM502 3.0 14.4 0.5
C1A A:HEM501 3.0 17.9 0.5
C4B A:HEM501 3.1 19.4 0.5
C1C A:HEM501 3.1 19.1 0.5
C4A A:HEM501 3.1 17.9 0.5
CZ A:TYR340 3.1 18.7 1.0
C1B A:HEM501 3.1 19.2 0.5
C4B A:HEM502 3.3 15.2 0.5
C1D A:HEM502 3.3 14.3 0.5
CHD A:HEM501 3.4 18.1 0.5
CHA A:HEM501 3.4 17.9 0.5
CHC A:HEM501 3.5 19.5 0.5
CHB A:HEM501 3.5 18.6 0.5
C3A A:HEM502 3.6 14.7 0.5
C2A A:HEM502 3.6 14.4 0.5
C4C A:HEM502 3.7 14.4 0.5
C1C A:HEM502 3.7 14.7 0.5
CE2 A:TYR340 3.7 19.4 1.0
CHC A:HEM502 3.9 15.1 0.5
CHD A:HEM502 4.0 14.3 0.5
CE1 A:TYR340 4.0 18.4 1.0
C2B A:HEM502 4.1 15.2 0.5
C2D A:HEM501 4.1 18.3 0.5
C3D A:HEM501 4.1 18.0 0.5
C3C A:HEM501 4.2 18.6 0.5
NH2 A:ARG336 4.2 21.4 1.0
C2C A:HEM501 4.2 19.4 0.5
C3A A:HEM501 4.2 17.2 0.5
C3D A:HEM502 4.2 14.1 0.5
C2A A:HEM501 4.2 17.2 0.5
NE2 A:HIS57 4.3 16.4 1.0
NE A:ARG336 4.3 20.2 1.0
C3B A:HEM501 4.3 19.4 0.5
C2B A:HEM501 4.3 19.6 0.5
C3B A:HEM502 4.3 15.5 0.5
O A:HOH1021 4.4 16.2 1.0
CD2 A:HIS57 4.4 16.3 1.0
C2D A:HEM502 4.4 14.1 0.5
CG2 A:VAL56 4.6 16.9 1.0
CZ A:ARG336 4.7 21.4 1.0
CZ A:PHE143 4.7 23.2 1.0
C2C A:HEM502 4.9 14.3 0.5
C3C A:HEM502 4.9 14.2 0.5
CMA A:HEM502 5.0 14.9 0.5

Iron binding site 2 out of 8 in 4qor

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Iron binding site 2 out of 8 in the Structure of Bacillus Pumilus Catalase with Chlorophenol 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 Chlorophenol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:15.4
occ:0.50
 FE A:HEM502 0.0 15.4 0.5
FE A:HEM501 0.7 20.6 0.5
NB A:HEM501 1.5 19.2 0.5
OH A:TYR340 1.9 18.9 1.0
ND A:HEM502 1.9 14.3 0.5
NA A:HEM502 2.0 14.7 0.5
NA A:HEM501 2.0 18.2 0.5
NB A:HEM502 2.1 14.8 0.5
NC A:HEM502 2.1 14.5 0.5
NC A:HEM501 2.2 18.8 0.5
C1B A:HEM501 2.5 19.2 0.5
C4B A:HEM501 2.5 19.4 0.5
ND A:HEM501 2.5 18.2 0.5
C4A A:HEM501 2.8 17.9 0.5
C1C A:HEM501 2.9 19.1 0.5
C4D A:HEM502 3.0 14.4 0.5
CZ A:TYR340 3.0 18.7 1.0
C1D A:HEM502 3.0 14.3 0.5
C4B A:HEM502 3.0 15.2 0.5
C1B A:HEM502 3.0 15.1 0.5
CHB A:HEM501 3.0 18.6 0.5
C1A A:HEM502 3.0 14.5 0.5
C4A A:HEM502 3.1 14.8 0.5
C4C A:HEM502 3.1 14.4 0.5
C1C A:HEM502 3.1 14.7 0.5
CHC A:HEM501 3.1 19.5 0.5
C1A A:HEM501 3.3 17.9 0.5
C4C A:HEM501 3.3 19.0 0.5
CHA A:HEM502 3.4 14.4 0.5
CHD A:HEM502 3.4 14.3 0.5
CHB A:HEM502 3.5 14.8 0.5
CHC A:HEM502 3.5 15.1 0.5
C4D A:HEM501 3.5 18.1 0.5
C1D A:HEM501 3.5 18.5 0.5
C2B A:HEM501 3.7 19.6 0.5
C3B A:HEM501 3.7 19.4 0.5
CE1 A:TYR340 3.7 18.4 1.0
CE2 A:TYR340 3.8 19.4 1.0
CHA A:HEM501 3.8 17.9 0.5
CHD A:HEM501 3.9 18.1 0.5
NE A:ARG336 4.0 20.2 1.0
C3A A:HEM501 4.1 17.2 0.5
C2C A:HEM501 4.2 19.4 0.5
C2B A:HEM502 4.2 15.2 0.5
C2A A:HEM502 4.2 14.4 0.5
C3A A:HEM502 4.2 14.7 0.5
NH2 A:ARG336 4.2 21.4 1.0
C2D A:HEM502 4.2 14.1 0.5
C3D A:HEM502 4.2 14.1 0.5
C3B A:HEM502 4.2 15.5 0.5
C3C A:HEM502 4.3 14.2 0.5
C2C A:HEM502 4.3 14.3 0.5
C2A A:HEM501 4.3 17.2 0.5
C3C A:HEM501 4.4 18.6 0.5
CZ A:PHE143 4.4 23.2 1.0
CZ A:ARG336 4.5 21.4 1.0
O A:HOH1021 4.6 16.2 1.0
CG2 A:VAL56 4.7 16.9 1.0
C3D A:HEM501 4.8 18.0 0.5
C2D A:HEM501 4.8 18.3 0.5
NE2 A:HIS57 4.8 16.4 1.0
CE2 A:PHE143 4.8 22.4 1.0
CD1 A:TYR340 4.9 17.2 1.0
CD2 A:HIS57 4.9 16.3 1.0
CD A:ARG336 5.0 19.8 1.0

Iron binding site 3 out of 8 in 4qor

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Iron binding site 3 out of 8 in the Structure of Bacillus Pumilus Catalase with Chlorophenol 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 Chlorophenol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:16.7
occ:0.50
 FE B:HEM501 0.0 16.7 0.5
FE B:HEM502 0.5 16.2 0.5
ND B:HEM501 1.9 14.6 0.5
NC B:HEM502 2.0 15.0 0.5
NA B:HEM501 2.0 14.9 0.5
NB B:HEM502 2.0 15.3 0.5
NB B:HEM501 2.1 15.4 0.5
NC B:HEM501 2.1 15.4 0.5
ND B:HEM502 2.1 14.8 0.5
O B:HOH977 2.1 23.6 1.0
NA B:HEM502 2.2 14.8 0.5
OH B:TYR340 2.3 13.7 1.0
C4D B:HEM501 2.9 14.8 0.5
C4B B:HEM502 2.9 15.6 0.5
C1D B:HEM501 2.9 15.0 0.5
C1C B:HEM502 2.9 15.5 0.5
C1A B:HEM501 3.0 14.3 0.5
C4B B:HEM501 3.0 15.9 0.5
C4C B:HEM502 3.0 14.7 0.5
C1B B:HEM501 3.0 15.0 0.5
C4C B:HEM501 3.0 15.3 0.5
C1D B:HEM502 3.1 14.4 0.5
C1B B:HEM502 3.1 15.1 0.5
C1C B:HEM501 3.1 15.9 0.5
C4D B:HEM502 3.1 14.2 0.5
C4A B:HEM501 3.1 14.5 0.5
C4A B:HEM502 3.2 15.1 0.5
C1A B:HEM502 3.2 14.8 0.5
CHC B:HEM502 3.3 15.3 0.5
CZ B:TYR340 3.3 15.1 1.0
CHA B:HEM501 3.4 14.4 0.5
CHD B:HEM501 3.4 14.8 0.5
CHC B:HEM501 3.5 15.7 0.5
CHD B:HEM502 3.5 14.1 0.5
CHB B:HEM501 3.5 14.3 0.5
CHB B:HEM502 3.6 14.8 0.5
CHA B:HEM502 3.6 14.6 0.5
CE2 B:TYR340 4.1 15.7 1.0
CE1 B:TYR340 4.1 15.7 1.0
C2C B:HEM502 4.2 15.4 0.5
C2D B:HEM501 4.2 14.7 0.5
C3C B:HEM502 4.2 14.8 0.5
C3D B:HEM501 4.2 14.3 0.5
C3B B:HEM502 4.2 15.3 0.5
C2B B:HEM501 4.2 15.4 0.5
C3C B:HEM501 4.2 15.4 0.5
C3B B:HEM501 4.2 15.8 0.5
C2A B:HEM501 4.2 14.0 0.5
C2B B:HEM502 4.2 15.2 0.5
C2C B:HEM501 4.2 15.6 0.5
CZ B:PHE143 4.3 21.2 1.0
C3A B:HEM501 4.3 14.2 0.5
O B:HOH978 4.3 16.1 1.0
NE B:ARG336 4.3 16.0 1.0
C2D B:HEM502 4.3 14.1 0.5
C3D B:HEM502 4.3 13.9 0.5
C3A B:HEM502 4.4 14.8 0.5
C2A B:HEM502 4.4 14.5 0.5
CG2 B:VAL56 4.4 13.7 1.0
NH2 B:ARG336 4.5 15.5 1.0
NE2 B:HIS57 4.5 14.4 1.0
CD2 B:HIS57 4.6 14.3 1.0
CE2 B:PHE143 4.8 19.7 1.0
CZ B:ARG336 4.8 16.1 1.0
CE1 B:PHE143 4.9 20.9 1.0

Iron binding site 4 out of 8 in 4qor

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Iron binding site 4 out of 8 in the Structure of Bacillus Pumilus Catalase with Chlorophenol 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 Chlorophenol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:16.2
occ:0.50
 FE B:HEM502 0.0 16.2 0.5
FE B:HEM501 0.5 16.7 0.5
ND B:HEM501 1.8 14.6 0.5
OH B:TYR340 1.8 13.7 1.0
ND B:HEM502 1.9 14.8 0.5
NA B:HEM501 2.0 14.9 0.5
NA B:HEM502 2.0 14.8 0.5
NB B:HEM502 2.1 15.3 0.5
NC B:HEM502 2.1 15.0 0.5
NC B:HEM501 2.2 15.4 0.5
NB B:HEM501 2.3 15.4 0.5
O B:HOH977 2.6 23.6 1.0
C4D B:HEM501 2.8 14.8 0.5
C1D B:HEM501 2.8 15.0 0.5
CZ B:TYR340 2.9 15.1 1.0
C1A B:HEM501 2.9 14.3 0.5
C4D B:HEM502 2.9 14.2 0.5
C1D B:HEM502 3.0 14.4 0.5
C1A B:HEM502 3.0 14.8 0.5
C4B B:HEM502 3.0 15.6 0.5
C4A B:HEM502 3.0 15.1 0.5
C4A B:HEM501 3.1 14.5 0.5
C4C B:HEM502 3.1 14.7 0.5
C1B B:HEM502 3.1 15.1 0.5
C4C B:HEM501 3.1 15.3 0.5
C1C B:HEM502 3.1 15.5 0.5
C1B B:HEM501 3.1 15.0 0.5
CHA B:HEM501 3.2 14.4 0.5
C4B B:HEM501 3.2 15.9 0.5
C1C B:HEM501 3.3 15.9 0.5
CHA B:HEM502 3.4 14.6 0.5
CHD B:HEM501 3.4 14.8 0.5
CHD B:HEM502 3.4 14.1 0.5
CHC B:HEM502 3.5 15.3 0.5
CHB B:HEM502 3.5 14.8 0.5
CHB B:HEM501 3.5 14.3 0.5
CE2 B:TYR340 3.6 15.7 1.0
CHC B:HEM501 3.7 15.7 0.5
CE1 B:TYR340 3.7 15.7 1.0
C2D B:HEM501 4.0 14.7 0.5
C3D B:HEM501 4.0 14.3 0.5
NE B:ARG336 4.1 16.0 1.0
C2A B:HEM501 4.1 14.0 0.5
NH2 B:ARG336 4.2 15.5 1.0
C3D B:HEM502 4.2 13.9 0.5
C3A B:HEM501 4.2 14.2 0.5
C2A B:HEM502 4.2 14.5 0.5
C3A B:HEM502 4.2 14.8 0.5
C2D B:HEM502 4.2 14.1 0.5
C3C B:HEM502 4.3 14.8 0.5
C3C B:HEM501 4.3 15.4 0.5
C2C B:HEM502 4.3 15.4 0.5
C2B B:HEM502 4.3 15.2 0.5
C3B B:HEM502 4.3 15.3 0.5
C2B B:HEM501 4.3 15.4 0.5
C2C B:HEM501 4.4 15.6 0.5
C3B B:HEM501 4.4 15.8 0.5
CZ B:ARG336 4.6 16.1 1.0
CG2 B:VAL56 4.7 13.7 1.0
O B:HOH978 4.7 16.1 1.0
CZ B:PHE143 4.7 21.2 1.0
NE2 B:HIS57 4.7 14.4 1.0
CD2 B:HIS57 4.8 14.3 1.0
CD2 B:TYR340 4.9 15.3 1.0
CD1 B:TYR340 4.9 15.5 1.0

Iron binding site 5 out of 8 in 4qor

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Iron binding site 5 out of 8 in the Structure of Bacillus Pumilus Catalase with Chlorophenol 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 Chlorophenol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:16.9
occ:0.50
 FE C:HEM501 0.0 16.9 0.5
FE C:HEM502 0.5 14.3 0.5
NA C:HEM502 1.8 13.1 0.5
ND C:HEM501 1.9 14.5 0.5
ND C:HEM502 1.9 13.1 0.5
NA C:HEM501 2.0 14.6 0.5
NB C:HEM501 2.1 14.6 0.5
NC C:HEM501 2.1 14.8 0.5
NB C:HEM502 2.2 13.2 0.5
OH C:TYR340 2.3 14.4 1.0
NC C:HEM502 2.4 13.0 0.5
C1A C:HEM502 2.8 12.9 0.5
C4D C:HEM502 2.8 13.1 0.5
C4A C:HEM502 2.8 13.0 0.5
C1D C:HEM501 2.9 14.6 0.5
C4D C:HEM501 2.9 14.4 0.5
C4C C:HEM501 3.0 14.9 0.5
C4A C:HEM501 3.0 14.8 0.5
C1B C:HEM501 3.0 14.8 0.5
C1A C:HEM501 3.0 14.6 0.5
C1D C:HEM502 3.0 13.2 0.5
C1B C:HEM502 3.0 13.4 0.5
C4B C:HEM501 3.1 14.7 0.5
C1C C:HEM501 3.2 14.9 0.5
CHA C:HEM502 3.2 13.0 0.5
C4B C:HEM502 3.3 13.3 0.5
CZ C:TYR340 3.3 13.7 1.0
CHB C:HEM502 3.3 13.1 0.5
C4C C:HEM502 3.3 13.1 0.5
CHD C:HEM501 3.3 14.6 0.5
CHA C:HEM501 3.4 14.4 0.5
C1C C:HEM502 3.4 12.9 0.5
CHB C:HEM501 3.4 14.7 0.5
CHC C:HEM501 3.6 14.5 0.5
CHD C:HEM502 3.6 13.1 0.5
CHC C:HEM502 3.8 12.8 0.5
CE2 C:TYR340 3.9 13.3 1.0
C2A C:HEM502 4.0 12.6 0.5
C3A C:HEM502 4.0 12.6 0.5
CE1 C:TYR340 4.1 13.2 1.0
C2D C:HEM501 4.1 14.1 0.5
C3D C:HEM502 4.1 13.1 0.5
C3D C:HEM501 4.2 14.0 0.5
C3C C:HEM501 4.2 14.8 0.5
C3A C:HEM501 4.2 14.5 0.5
C2D C:HEM502 4.2 13.1 0.5
C2A C:HEM501 4.3 14.4 0.5
C2B C:HEM501 4.3 14.2 0.5
C2C C:HEM501 4.3 14.8 0.5
C3B C:HEM501 4.3 14.4 0.5
NE2 C:HIS57 4.3 13.5 1.0
C2B C:HEM502 4.3 13.2 0.5
CG2 C:VAL56 4.3 14.8 1.0
NE C:ARG336 4.4 15.9 1.0
CD2 C:HIS57 4.4 13.4 1.0
C3B C:HEM502 4.4 13.2 0.5
NH2 C:ARG336 4.4 15.9 1.0
O C:HOH987 4.4 20.1 1.0
CZ C:PHE143 4.5 15.7 1.0
C3C C:HEM502 4.5 12.4 0.5
C2C C:HEM502 4.6 12.6 0.5
CZ C:ARG336 4.8 15.9 1.0
CE2 C:PHE143 4.9 15.7 1.0

Iron binding site 6 out of 8 in 4qor

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Iron binding site 6 out of 8 in the Structure of Bacillus Pumilus Catalase with Chlorophenol 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 Chlorophenol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe502

b:14.3
occ:0.50
 FE C:HEM502 0.0 14.3 0.5
FE C:HEM501 0.5 16.9 0.5
NB C:HEM501 1.8 14.6 0.5
OH C:TYR340 1.8 14.4 1.0
ND C:HEM502 1.9 13.1 0.5
NA C:HEM502 2.0 13.1 0.5
NC C:HEM502 2.0 13.0 0.5
NB C:HEM502 2.1 13.2 0.5
NC C:HEM501 2.1 14.8 0.5
NA C:HEM501 2.1 14.6 0.5
ND C:HEM501 2.2 14.5 0.5
C1B C:HEM501 2.8 14.8 0.5
C4B C:HEM501 2.8 14.7 0.5
CZ C:TYR340 2.9 13.7 1.0
C1D C:HEM502 2.9 13.2 0.5
C4D C:HEM502 3.0 13.1 0.5
C4A C:HEM501 3.0 14.8 0.5
C4C C:HEM502 3.0 13.1 0.5
C1C C:HEM501 3.0 14.9 0.5
C1B C:HEM502 3.0 13.4 0.5
C4A C:HEM502 3.0 13.0 0.5
C1A C:HEM502 3.1 12.9 0.5
C4B C:HEM502 3.1 13.3 0.5
C1C C:HEM502 3.1 12.9 0.5
C4C C:HEM501 3.1 14.9 0.5
C1D C:HEM501 3.2 14.6 0.5
C1A C:HEM501 3.2 14.6 0.5
C4D C:HEM501 3.2 14.4 0.5
CHB C:HEM501 3.3 14.7 0.5
CHC C:HEM501 3.4 14.5 0.5
CHD C:HEM502 3.4 13.1 0.5
CHB C:HEM502 3.4 13.1 0.5
CHA C:HEM502 3.5 13.0 0.5
CHC C:HEM502 3.5 12.8 0.5
CHD C:HEM501 3.5 14.6 0.5
CE1 C:TYR340 3.6 13.2 1.0
CE2 C:TYR340 3.7 13.3 1.0
CHA C:HEM501 3.7 14.4 0.5
NE C:ARG336 3.9 15.9 1.0
C2B C:HEM501 4.0 14.2 0.5
C3B C:HEM501 4.0 14.4 0.5
NH2 C:ARG336 4.1 15.9 1.0
C2C C:HEM501 4.2 14.8 0.5
C3C C:HEM502 4.2 12.4 0.5
C2D C:HEM502 4.2 13.1 0.5
C3C C:HEM501 4.2 14.8 0.5
C3D C:HEM502 4.2 13.1 0.5
C2C C:HEM502 4.2 12.6 0.5
C3A C:HEM501 4.2 14.5 0.5
C3A C:HEM502 4.2 12.6 0.5
C2A C:HEM502 4.2 12.6 0.5
C2B C:HEM502 4.3 13.2 0.5
C3B C:HEM502 4.3 13.2 0.5
C2A C:HEM501 4.3 14.4 0.5
C2D C:HEM501 4.4 14.1 0.5
CZ C:ARG336 4.5 15.9 1.0
C3D C:HEM501 4.5 14.0 0.5
CZ C:PHE143 4.6 15.7 1.0
CG2 C:VAL56 4.7 14.8 1.0
NE2 C:HIS57 4.8 13.5 1.0
O C:HOH987 4.8 20.1 1.0
CD1 C:TYR340 4.9 13.4 1.0
CD2 C:TYR340 4.9 13.4 1.0
CD2 C:HIS57 4.9 13.4 1.0
CD C:ARG336 4.9 15.8 1.0
CE2 C:PHE143 5.0 15.7 1.0

Iron binding site 7 out of 8 in 4qor

Go back to Iron Binding Sites List in 4qor
Iron binding site 7 out of 8 in the Structure of Bacillus Pumilus Catalase with Chlorophenol 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 Chlorophenol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:23.6
occ:0.50
 FE D:HEM501 0.0 23.6 0.5
FE D:HEM502 0.6 13.9 0.5
ND D:HEM501 1.9 19.4 0.5
NB D:HEM502 2.0 13.3 0.5
NA D:HEM501 2.0 19.9 0.5
NC D:HEM501 2.1 20.3 0.5
NB D:HEM501 2.1 20.4 0.5
NA D:HEM502 2.1 13.1 0.5
NC D:HEM502 2.1 13.0 0.5
ND D:HEM502 2.1 13.1 0.5
OH D:TYR340 2.3 15.3 1.0
C1D D:HEM501 2.9 19.1 0.5
C4B D:HEM502 2.9 13.4 0.5
O D:HOH975 2.9 34.5 1.0
C4D D:HEM501 2.9 19.4 0.5
C1B D:HEM502 3.0 13.6 0.5
C4C D:HEM501 3.0 20.4 0.5
C4B D:HEM501 3.0 20.6 0.5
C4A D:HEM502 3.0 13.1 0.5
C1C D:HEM502 3.0 13.3 0.5
C1A D:HEM501 3.0 19.8 0.5
C1B D:HEM501 3.1 20.3 0.5
C4A D:HEM501 3.1 20.4 0.5
C1C D:HEM501 3.1 20.6 0.5
C1A D:HEM502 3.1 13.1 0.5
C4D D:HEM502 3.1 12.9 0.5
C1D D:HEM502 3.2 13.1 0.5
C4C D:HEM502 3.2 13.0 0.5
CHC D:HEM502 3.3 13.4 0.5
CHD D:HEM501 3.4 19.8 0.5
CZ D:TYR340 3.4 15.7 1.0
CHB D:HEM502 3.4 13.3 0.5
CHA D:HEM501 3.4 19.4 0.5
CHC D:HEM501 3.5 20.7 0.5
CHB D:HEM501 3.5 19.7 0.5
CHA D:HEM502 3.6 12.9 0.5
CHD D:HEM502 3.6 12.8 0.5
CE2 D:TYR340 4.1 14.8 1.0
C2D D:HEM501 4.1 18.6 0.5
C3B D:HEM502 4.1 13.2 0.5
C2B D:HEM502 4.1 13.5 0.5
C3D D:HEM501 4.2 18.5 0.5
C3C D:HEM501 4.2 20.3 0.5
C2C D:HEM501 4.2 20.2 0.5
CE1 D:TYR340 4.2 15.3 1.0
C3A D:HEM502 4.2 12.9 0.5
C3B D:HEM501 4.2 20.5 0.5
C2B D:HEM501 4.2 19.7 0.5
C2A D:HEM501 4.3 19.6 0.5
C3A D:HEM501 4.3 19.7 0.5
C2C D:HEM502 4.3 13.1 0.5
O D:HOH973 4.3 16.5 1.0
C2A D:HEM502 4.3 12.8 0.5
CZ D:PHE143 4.3 19.6 1.0
NE D:ARG336 4.3 19.8 1.0
C3C D:HEM502 4.3 12.8 0.5
NE2 D:HIS57 4.4 17.2 1.0
CG2 D:VAL56 4.4 15.4 1.0
C3D D:HEM502 4.4 12.7 0.5
C2D D:HEM502 4.4 12.8 0.5
NH2 D:ARG336 4.4 21.4 1.0
CD2 D:HIS57 4.5 16.6 1.0
CZ D:ARG336 4.8 20.1 1.0
CE2 D:PHE143 4.9 19.5 1.0
CE1 D:PHE143 5.0 19.5 1.0

Iron binding site 8 out of 8 in 4qor

Go back to Iron Binding Sites List in 4qor
Iron binding site 8 out of 8 in the Structure of Bacillus Pumilus Catalase with Chlorophenol 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 Chlorophenol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe502

b:13.9
occ:0.50
 FE D:HEM502 0.0 13.9 0.5
FE D:HEM501 0.6 23.6 0.5
OH D:TYR340 1.8 15.3 1.0
ND D:HEM502 1.9 13.1 0.5
NA D:HEM501 1.9 19.9 0.5
ND D:HEM501 2.0 19.4 0.5
NA D:HEM502 2.0 13.1 0.5
NC D:HEM502 2.1 13.0 0.5
NB D:HEM502 2.1 13.3 0.5
NB D:HEM501 2.1 20.4 0.5
NC D:HEM501 2.3 20.3 0.5
CZ D:TYR340 2.8 15.7 1.0
C4D D:HEM501 2.9 19.4 0.5
C4A D:HEM501 2.9 20.4 0.5
C1A D:HEM501 2.9 19.8 0.5
C1D D:HEM502 2.9 13.1 0.5
C4D D:HEM502 2.9 12.9 0.5
C1D D:HEM501 2.9 19.1 0.5
C1B D:HEM501 3.0 20.3 0.5
C4B D:HEM502 3.0 13.4 0.5
C4A D:HEM502 3.0 13.1 0.5
C1A D:HEM502 3.0 13.1 0.5
C4C D:HEM502 3.1 13.0 0.5
C1B D:HEM502 3.1 13.6 0.5
C1C D:HEM502 3.1 13.3 0.5
C4B D:HEM501 3.1 20.6 0.5
C4C D:HEM501 3.2 20.4 0.5
C1C D:HEM501 3.3 20.6 0.5
CHA D:HEM501 3.3 19.4 0.5
CHB D:HEM501 3.3 19.7 0.5
CHA D:HEM502 3.4 12.9 0.5
CHD D:HEM502 3.4 12.8 0.5
CHC D:HEM502 3.4 13.4 0.5
CHB D:HEM502 3.5 13.3 0.5
O D:HOH975 3.5 34.5 1.0
CHD D:HEM501 3.5 19.8 0.5
CE2 D:TYR340 3.5 14.8 1.0
CE1 D:TYR340 3.7 15.3 1.0
CHC D:HEM501 3.7 20.7 0.5
NE D:ARG336 4.0 19.8 1.0
C3A D:HEM501 4.1 19.7 0.5
C2A D:HEM501 4.1 19.6 0.5
NH2 D:ARG336 4.1 21.4 1.0
C3D D:HEM501 4.1 18.5 0.5
C2D D:HEM501 4.1 18.6 0.5
C2D D:HEM502 4.2 12.8 0.5
C3D D:HEM502 4.2 12.7 0.5
C3A D:HEM502 4.2 12.9 0.5
C2B D:HEM501 4.2 19.7 0.5
C2A D:HEM502 4.3 12.8 0.5
C3C D:HEM502 4.3 12.8 0.5
C2C D:HEM502 4.3 13.1 0.5
C2B D:HEM502 4.3 13.5 0.5
C3B D:HEM502 4.3 13.2 0.5
C3B D:HEM501 4.3 20.5 0.5
C3C D:HEM501 4.3 20.3 0.5
C2C D:HEM501 4.4 20.2 0.5
CZ D:ARG336 4.5 20.1 1.0
CG2 D:VAL56 4.7 15.4 1.0
CZ D:PHE143 4.7 19.6 1.0
NE2 D:HIS57 4.8 17.2 1.0
CD2 D:TYR340 4.8 15.0 1.0
O D:HOH973 4.9 16.5 1.0
CD2 D:HIS57 4.9 16.6 1.0
CD1 D:TYR340 4.9 15.5 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: Mon Aug 5 08:58:55 2024

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