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Iron in PDB 4qol: Structure of Bacillus Pumilus Catalase

Enzymatic activity of Structure of Bacillus Pumilus Catalase

All present enzymatic activity of Structure of Bacillus Pumilus Catalase:
1.11.1.6;

Protein crystallography data

The structure of Structure of Bacillus Pumilus Catalase, PDB code: 4qol 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) 102.79 / 1.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 91.647, 109.191, 102.829, 90.00, 91.67, 90.00
R / Rfree (%) 17.1 / 19.9

Other elements in 4qol:

The structure of Structure of Bacillus Pumilus Catalase 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 (pdb code 4qol). 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, PDB code: 4qol:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 4qol

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Iron binding site 1 out of 8 in the Structure of Bacillus Pumilus Catalase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:14.6
occ:0.50
 FE A:HEM501 0.0 14.6 0.5
FE A:HEM502 0.6 13.0 0.5
NA A:HEM502 1.5 11.0 0.5
ND A:HEM501 1.9 11.8 0.5
ND A:HEM502 1.9 11.2 0.5
OH A:TYR340 2.0 12.7 1.0
NA A:HEM501 2.0 12.8 0.5
NC A:HEM501 2.1 12.3 0.5
NB A:HEM501 2.1 11.6 0.5
NB A:HEM502 2.2 11.2 0.5
C1A A:HEM502 2.5 10.8 0.5
C4A A:HEM502 2.5 10.4 0.5
NC A:HEM502 2.6 10.8 0.5
C4D A:HEM502 2.8 10.7 0.5
C1D A:HEM501 2.9 11.4 0.5
C4D A:HEM501 3.0 11.5 0.5
CZ A:TYR340 3.0 12.2 1.0
C1B A:HEM502 3.0 10.6 0.5
CHA A:HEM502 3.0 10.5 0.5
C4C A:HEM501 3.0 12.0 0.5
C1B A:HEM501 3.0 11.7 0.5
C4B A:HEM501 3.0 11.4 0.5
C1A A:HEM501 3.1 11.9 0.5
C1C A:HEM501 3.1 11.9 0.5
C4A A:HEM501 3.1 11.6 0.5
CHB A:HEM502 3.1 10.4 0.5
C1D A:HEM502 3.2 10.4 0.5
C4B A:HEM502 3.4 10.9 0.5
CHD A:HEM501 3.4 11.7 0.5
CHA A:HEM501 3.4 11.4 0.5
CHB A:HEM501 3.5 11.4 0.5
CHC A:HEM501 3.5 11.7 0.5
C4C A:HEM502 3.6 10.7 0.5
CE2 A:TYR340 3.6 12.4 1.0
C1C A:HEM502 3.6 10.5 0.5
C3A A:HEM502 3.7 10.1 0.5
C2A A:HEM502 3.7 10.3 0.5
CHD A:HEM502 3.8 10.4 0.5
CE1 A:TYR340 3.8 12.0 1.0
CHC A:HEM502 3.9 10.7 0.5
C2D A:HEM501 4.2 11.1 0.5
C3D A:HEM502 4.2 10.3 0.5
C3C A:HEM501 4.2 11.7 0.5
C3D A:HEM501 4.2 10.6 0.5
NH2 A:ARG336 4.2 11.9 1.0
C2C A:HEM501 4.2 12.1 0.5
C2B A:HEM501 4.2 11.5 0.5
C2B A:HEM502 4.3 10.5 0.5
C3B A:HEM501 4.3 11.3 0.5
C2A A:HEM501 4.3 12.0 0.5
C3A A:HEM501 4.3 11.8 0.5
NE A:ARG336 4.3 12.7 1.0
C2D A:HEM502 4.4 10.2 0.5
O A:HOH1036 4.4 19.4 1.0
NE2 A:HIS57 4.4 13.2 1.0
C3B A:HEM502 4.5 11.0 0.5
CD2 A:HIS57 4.5 11.6 1.0
CG2 A:VAL56 4.6 13.0 1.0
CZ A:ARG336 4.7 12.4 1.0
CZ A:PHE143 4.7 13.3 1.0
C3C A:HEM502 4.8 10.5 0.5
C2C A:HEM502 4.8 10.6 0.5
CD2 A:TYR340 4.9 13.0 1.0

Iron binding site 2 out of 8 in 4qol

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Iron binding site 2 out of 8 in the Structure of Bacillus Pumilus Catalase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:13.0
occ:0.50
 FE A:HEM502 0.0 13.0 0.5
FE A:HEM501 0.6 14.6 0.5
NB A:HEM501 1.5 11.6 0.5
ND A:HEM502 1.9 11.2 0.5
OH A:TYR340 2.0 12.7 1.0
NA A:HEM502 2.0 11.0 0.5
NC A:HEM502 2.1 10.8 0.5
NC A:HEM501 2.1 12.3 0.5
NB A:HEM502 2.1 11.2 0.5
NA A:HEM501 2.1 12.8 0.5
ND A:HEM501 2.5 11.8 0.5
C4B A:HEM501 2.5 11.4 0.5
C1B A:HEM501 2.5 11.7 0.5
C1C A:HEM501 2.9 11.9 0.5
CZ A:TYR340 3.0 12.2 1.0
C4A A:HEM501 3.0 11.6 0.5
C1D A:HEM502 3.0 10.4 0.5
C4D A:HEM502 3.0 10.7 0.5
C4A A:HEM502 3.0 10.4 0.5
C4B A:HEM502 3.0 10.9 0.5
C4C A:HEM502 3.1 10.7 0.5
C1A A:HEM502 3.1 10.8 0.5
C1B A:HEM502 3.1 10.6 0.5
C1C A:HEM502 3.1 10.5 0.5
CHC A:HEM501 3.1 11.7 0.5
CHB A:HEM501 3.2 11.4 0.5
C4C A:HEM501 3.2 12.0 0.5
C1A A:HEM501 3.3 11.9 0.5
C1D A:HEM501 3.4 11.4 0.5
CHD A:HEM502 3.4 10.4 0.5
CHA A:HEM502 3.4 10.5 0.5
CHB A:HEM502 3.4 10.4 0.5
CHC A:HEM502 3.4 10.7 0.5
C4D A:HEM501 3.5 11.5 0.5
CE1 A:TYR340 3.7 12.0 1.0
C2B A:HEM501 3.7 11.5 0.5
C3B A:HEM501 3.7 11.3 0.5
CHD A:HEM501 3.8 11.7 0.5
CE2 A:TYR340 3.8 12.4 1.0
CHA A:HEM501 3.9 11.4 0.5
NE A:ARG336 4.1 12.7 1.0
C2C A:HEM501 4.1 12.1 0.5
C3A A:HEM502 4.2 10.1 0.5
C3C A:HEM502 4.2 10.5 0.5
C2C A:HEM502 4.2 10.6 0.5
C2B A:HEM502 4.3 10.5 0.5
C2A A:HEM502 4.3 10.3 0.5
C3C A:HEM501 4.3 11.7 0.5
C3B A:HEM502 4.3 11.0 0.5
C2D A:HEM502 4.3 10.2 0.5
NH2 A:ARG336 4.3 11.9 1.0
C3A A:HEM501 4.3 11.8 0.5
C3D A:HEM502 4.3 10.3 0.5
CZ A:PHE143 4.4 13.3 1.0
C2A A:HEM501 4.5 12.0 0.5
O A:HOH1036 4.5 19.4 1.0
CZ A:ARG336 4.6 12.4 1.0
CG2 A:VAL56 4.7 13.0 1.0
C2D A:HEM501 4.7 11.1 0.5
C3D A:HEM501 4.8 10.6 0.5
NE2 A:HIS57 4.8 13.2 1.0
CE2 A:PHE143 4.8 12.6 1.0
CD1 A:TYR340 4.9 12.5 1.0
CD2 A:HIS57 4.9 11.6 1.0
CE1 A:PHE143 4.9 12.4 1.0
CD A:ARG336 5.0 12.8 1.0

Iron binding site 3 out of 8 in 4qol

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Iron binding site 3 out of 8 in the Structure of Bacillus Pumilus Catalase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:18.6
occ:0.50
 FE B:HEM501 0.0 18.6 0.5
FE B:HEM502 0.4 12.8 0.5
ND B:HEM502 1.9 11.7 0.5
ND B:HEM501 1.9 14.0 0.5
NC B:HEM502 2.0 11.9 0.5
NA B:HEM501 2.0 14.2 0.5
NB B:HEM501 2.1 14.6 0.5
NC B:HEM501 2.1 13.8 0.5
O B:HOH990 2.1 27.5 1.0
NA B:HEM502 2.2 12.0 0.5
OH B:TYR340 2.2 13.4 1.0
NB B:HEM502 2.2 11.9 0.5
C1D B:HEM502 2.8 11.2 0.5
C4C B:HEM502 2.9 11.7 0.5
C4D B:HEM501 2.9 13.0 0.5
C1D B:HEM501 2.9 13.3 0.5
C4D B:HEM502 2.9 11.2 0.5
C4B B:HEM501 3.0 14.7 0.5
C1C B:HEM502 3.0 12.2 0.5
C1B B:HEM501 3.0 14.4 0.5
C1A B:HEM501 3.0 13.6 0.5
C4C B:HEM501 3.1 13.4 0.5
C4A B:HEM501 3.1 13.3 0.5
C4B B:HEM502 3.1 12.0 0.5
C1A B:HEM502 3.1 10.8 0.5
C1C B:HEM501 3.1 13.9 0.5
CZ B:TYR340 3.2 11.5 1.0
CHD B:HEM502 3.2 11.1 0.5
C4A B:HEM502 3.2 11.2 0.5
C1B B:HEM502 3.3 11.6 0.5
CHA B:HEM501 3.4 13.0 0.5
CHD B:HEM501 3.4 13.7 0.5
CHB B:HEM501 3.4 13.8 0.5
CHC B:HEM502 3.4 11.8 0.5
CHA B:HEM502 3.4 10.9 0.5
CHC B:HEM501 3.5 13.7 0.5
CHB B:HEM502 3.7 11.9 0.5
CE2 B:TYR340 3.9 11.6 1.0
CE1 B:TYR340 3.9 11.6 1.0
C3C B:HEM502 4.1 11.5 0.5
C2D B:HEM502 4.1 10.9 0.5
C3D B:HEM502 4.2 10.6 0.5
C2C B:HEM502 4.2 12.0 0.5
C2D B:HEM501 4.2 12.7 0.5
C3D B:HEM501 4.2 12.0 0.5
C2A B:HEM501 4.2 12.8 0.5
C3B B:HEM501 4.2 14.4 0.5
C2B B:HEM501 4.3 14.2 0.5
CZ B:PHE143 4.3 13.7 1.0
C3C B:HEM501 4.3 13.8 0.5
C2C B:HEM501 4.3 13.6 0.5
NE B:ARG336 4.3 13.5 1.0
C3A B:HEM501 4.3 13.1 0.5
C2A B:HEM502 4.4 10.4 0.5
C3B B:HEM502 4.4 11.8 0.5
CG2 B:VAL56 4.4 12.5 1.0
C3A B:HEM502 4.4 10.8 0.5
NH2 B:ARG336 4.4 13.3 1.0
C2B B:HEM502 4.4 11.9 0.5
O B:HOH991 4.5 20.1 1.0
NE2 B:HIS57 4.5 12.5 1.0
CD2 B:HIS57 4.6 12.4 1.0
CE2 B:PHE143 4.7 11.9 1.0
CZ B:ARG336 4.8 14.2 1.0
CE1 B:PHE143 4.9 12.8 1.0

Iron binding site 4 out of 8 in 4qol

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Iron binding site 4 out of 8 in the Structure of Bacillus Pumilus Catalase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:12.8
occ:0.50
 FE B:HEM502 0.0 12.8 0.5
FE B:HEM501 0.4 18.6 0.5
ND B:HEM501 1.8 14.0 0.5
OH B:TYR340 1.9 13.4 1.0
ND B:HEM502 1.9 11.7 0.5
NA B:HEM502 2.0 12.0 0.5
NC B:HEM501 2.0 13.8 0.5
NB B:HEM502 2.1 11.9 0.5
NC B:HEM502 2.1 11.9 0.5
NA B:HEM501 2.2 14.2 0.5
NB B:HEM501 2.3 14.6 0.5
O B:HOH990 2.4 27.5 1.0
C1D B:HEM501 2.7 13.3 0.5
C4D B:HEM501 2.8 13.0 0.5
C4C B:HEM501 2.9 13.4 0.5
CZ B:TYR340 2.9 11.5 1.0
C4D B:HEM502 3.0 11.2 0.5
C1D B:HEM502 3.0 11.2 0.5
C1A B:HEM502 3.0 10.8 0.5
C4A B:HEM502 3.0 11.2 0.5
C4B B:HEM502 3.0 12.0 0.5
C1B B:HEM502 3.0 11.6 0.5
C4C B:HEM502 3.1 11.7 0.5
C1C B:HEM501 3.1 13.9 0.5
C1C B:HEM502 3.1 12.2 0.5
C1A B:HEM501 3.1 13.6 0.5
C4B B:HEM501 3.1 14.7 0.5
CHD B:HEM501 3.2 13.7 0.5
C1B B:HEM501 3.2 14.4 0.5
C4A B:HEM501 3.3 13.3 0.5
CHD B:HEM502 3.4 11.1 0.5
CHA B:HEM501 3.4 13.0 0.5
CHB B:HEM502 3.4 11.9 0.5
CHA B:HEM502 3.4 10.9 0.5
CHC B:HEM502 3.5 11.8 0.5
CHC B:HEM501 3.5 13.7 0.5
CE2 B:TYR340 3.6 11.6 1.0
CHB B:HEM501 3.6 13.8 0.5
CE1 B:TYR340 3.7 11.6 1.0
C2D B:HEM501 4.0 12.7 0.5
NE B:ARG336 4.0 13.5 1.0
NH2 B:ARG336 4.1 13.3 1.0
C3D B:HEM501 4.1 12.0 0.5
C3C B:HEM501 4.1 13.8 0.5
C2C B:HEM501 4.2 13.6 0.5
C3A B:HEM502 4.2 10.8 0.5
C2A B:HEM502 4.2 10.4 0.5
C3D B:HEM502 4.3 10.6 0.5
C3C B:HEM502 4.3 11.5 0.5
C2B B:HEM502 4.3 11.9 0.5
C3B B:HEM502 4.3 11.8 0.5
C2D B:HEM502 4.3 10.9 0.5
C2C B:HEM502 4.3 12.0 0.5
C2A B:HEM501 4.3 12.8 0.5
C3B B:HEM501 4.4 14.4 0.5
C2B B:HEM501 4.4 14.2 0.5
C3A B:HEM501 4.5 13.1 0.5
CZ B:ARG336 4.5 14.2 1.0
NE2 B:HIS57 4.6 12.5 1.0
CZ B:PHE143 4.6 13.7 1.0
O B:HOH991 4.7 20.1 1.0
CG2 B:VAL56 4.7 12.5 1.0
CD2 B:HIS57 4.7 12.4 1.0
CD2 B:TYR340 4.9 12.2 1.0
CD1 B:TYR340 5.0 12.5 1.0

Iron binding site 5 out of 8 in 4qol

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Iron binding site 5 out of 8 in the Structure of Bacillus Pumilus Catalase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:17.5
occ:0.50
 FE C:HEM501 0.0 17.5 0.5
FE C:HEM502 0.5 9.2 0.5
ND C:HEM501 1.9 12.6 0.5
ND C:HEM502 1.9 8.9 0.5
NA C:HEM502 2.0 8.8 0.5
NA C:HEM501 2.0 12.8 0.5
NC C:HEM501 2.1 14.2 0.5
NB C:HEM501 2.1 13.4 0.5
O C:HOH997 2.1 25.9 1.0
NC C:HEM502 2.2 8.8 0.5
NB C:HEM502 2.2 9.5 0.5
OH C:TYR340 2.3 10.1 1.0
C1D C:HEM501 2.9 13.0 0.5
C4D C:HEM502 2.9 8.5 0.5
C4D C:HEM501 2.9 12.9 0.5
C1A C:HEM502 3.0 8.9 0.5
C1D C:HEM502 3.0 8.5 0.5
C4B C:HEM501 3.0 14.5 0.5
C4C C:HEM501 3.0 14.0 0.5
C1A C:HEM501 3.0 12.4 0.5
C1B C:HEM501 3.0 14.0 0.5
C4A C:HEM502 3.1 8.8 0.5
C1C C:HEM501 3.1 14.5 0.5
C4A C:HEM501 3.1 12.3 0.5
C1B C:HEM502 3.1 9.2 0.5
C4B C:HEM502 3.1 9.6 0.5
C4C C:HEM502 3.2 8.8 0.5
C1C C:HEM502 3.2 9.2 0.5
CZ C:TYR340 3.3 10.1 1.0
CHA C:HEM502 3.3 8.5 0.5
CHA C:HEM501 3.4 12.3 0.5
CHD C:HEM501 3.4 12.6 0.5
CHC C:HEM501 3.5 14.5 0.5
CHB C:HEM502 3.5 8.8 0.5
CHB C:HEM501 3.5 12.8 0.5
CHD C:HEM502 3.5 8.7 0.5
CHC C:HEM502 3.5 9.5 0.5
CE2 C:TYR340 4.0 10.2 1.0
CE1 C:TYR340 4.1 9.5 1.0
C2D C:HEM501 4.1 12.1 0.5
C2A C:HEM502 4.2 8.3 0.5
C3D C:HEM501 4.2 11.6 0.5
C3C C:HEM501 4.2 14.4 0.5
C3A C:HEM502 4.2 8.6 0.5
C3D C:HEM502 4.2 8.7 0.5
C2B C:HEM501 4.2 13.5 0.5
C2D C:HEM502 4.2 8.7 0.5
C3B C:HEM501 4.2 13.8 0.5
CG2 C:VAL56 4.3 11.0 1.0
C2C C:HEM501 4.3 14.9 0.5
CZ C:PHE143 4.3 12.8 1.0
C2A C:HEM501 4.3 12.3 0.5
C3A C:HEM501 4.3 12.4 0.5
NE2 C:HIS57 4.3 10.7 1.0
O C:HOH995 4.3 16.1 1.0
C3C C:HEM502 4.3 8.5 0.5
C2B C:HEM502 4.4 9.4 0.5
C2C C:HEM502 4.4 8.8 0.5
C3B C:HEM502 4.4 9.9 0.5
NE C:ARG336 4.4 12.4 1.0
CD2 C:HIS57 4.4 9.9 1.0
NH2 C:ARG336 4.5 13.3 1.0
CE2 C:PHE143 4.8 12.7 1.0
CZ C:ARG336 4.8 13.2 1.0
CE1 C:PHE143 4.9 13.8 1.0

Iron binding site 6 out of 8 in 4qol

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Iron binding site 6 out of 8 in the Structure of Bacillus Pumilus Catalase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe502

b:9.2
occ:0.50
 FE C:HEM502 0.0 9.2 0.5
FE C:HEM501 0.5 17.5 0.5
OH C:TYR340 1.8 10.1 1.0
ND C:HEM502 1.9 8.9 0.5
NA C:HEM502 2.0 8.8 0.5
ND C:HEM501 2.0 12.6 0.5
NB C:HEM501 2.0 13.4 0.5
NC C:HEM502 2.1 8.8 0.5
NC C:HEM501 2.1 14.2 0.5
NB C:HEM502 2.1 9.5 0.5
NA C:HEM501 2.1 12.8 0.5
O C:HOH997 2.6 25.9 1.0
CZ C:TYR340 2.8 10.1 1.0
C1D C:HEM501 3.0 13.0 0.5
C4B C:HEM501 3.0 14.5 0.5
C4D C:HEM502 3.0 8.5 0.5
C1D C:HEM502 3.0 8.5 0.5
C4C C:HEM501 3.0 14.0 0.5
C1B C:HEM501 3.0 14.0 0.5
C1A C:HEM502 3.0 8.9 0.5
C1B C:HEM502 3.0 9.2 0.5
C4D C:HEM501 3.0 12.9 0.5
C4B C:HEM502 3.0 9.6 0.5
C4A C:HEM502 3.1 8.8 0.5
C4C C:HEM502 3.1 8.8 0.5
C1C C:HEM501 3.1 14.5 0.5
C1C C:HEM502 3.1 9.2 0.5
C4A C:HEM501 3.1 12.3 0.5
C1A C:HEM501 3.1 12.4 0.5
CHA C:HEM502 3.4 8.5 0.5
CHD C:HEM501 3.4 12.6 0.5
CHC C:HEM501 3.4 14.5 0.5
CHB C:HEM502 3.4 8.8 0.5
CHD C:HEM502 3.5 8.7 0.5
CHC C:HEM502 3.5 9.5 0.5
CHB C:HEM501 3.5 12.8 0.5
CHA C:HEM501 3.5 12.3 0.5
CE1 C:TYR340 3.6 9.5 1.0
CE2 C:TYR340 3.6 10.2 1.0
NE C:ARG336 3.9 12.4 1.0
NH2 C:ARG336 4.1 13.3 1.0
C3C C:HEM501 4.1 14.4 0.5
C2B C:HEM501 4.2 13.5 0.5
C3B C:HEM501 4.2 13.8 0.5
C2C C:HEM501 4.2 14.9 0.5
C2D C:HEM501 4.2 12.1 0.5
C3A C:HEM502 4.2 8.6 0.5
C3C C:HEM502 4.2 8.5 0.5
C2D C:HEM502 4.2 8.7 0.5
C2A C:HEM502 4.2 8.3 0.5
C3D C:HEM502 4.2 8.7 0.5
C2C C:HEM502 4.3 8.8 0.5
C3D C:HEM501 4.3 11.6 0.5
C2B C:HEM502 4.3 9.4 0.5
C3B C:HEM502 4.3 9.9 0.5
C3A C:HEM501 4.3 12.4 0.5
C2A C:HEM501 4.3 12.3 0.5
CZ C:ARG336 4.4 13.2 1.0
CZ C:PHE143 4.6 12.8 1.0
CG2 C:VAL56 4.7 11.0 1.0
NE2 C:HIS57 4.7 10.7 1.0
O C:HOH995 4.7 16.1 1.0
CD2 C:HIS57 4.8 9.9 1.0
CD1 C:TYR340 4.8 9.7 1.0
CD2 C:TYR340 4.9 9.8 1.0
CD C:ARG336 5.0 12.4 1.0

Iron binding site 7 out of 8 in 4qol

Go back to Iron Binding Sites List in 4qol
Iron binding site 7 out of 8 in the Structure of Bacillus Pumilus Catalase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:20.9
occ:0.50
 FE D:HEM501 0.0 20.9 0.5
FE D:HEM502 0.6 9.8 0.5
ND D:HEM501 1.9 16.1 0.5
NB D:HEM502 2.0 9.9 0.5
NA D:HEM501 2.0 15.0 0.5
NC D:HEM501 2.1 15.7 0.5
NB D:HEM501 2.1 17.5 0.5
NC D:HEM502 2.1 9.9 0.5
ND D:HEM502 2.1 9.0 0.5
NA D:HEM502 2.2 9.6 0.5
OH D:TYR340 2.4 15.8 1.0
O D:HOH993 2.4 28.2 1.0
C4B D:HEM502 2.9 10.1 0.5
C1D D:HEM501 2.9 15.5 0.5
C4D D:HEM501 3.0 15.5 0.5
C4C D:HEM501 3.0 16.5 0.5
C4B D:HEM501 3.0 16.8 0.5
C1C D:HEM502 3.0 9.9 0.5
C1B D:HEM502 3.0 10.0 0.5
C1B D:HEM501 3.0 15.9 0.5
C1A D:HEM501 3.1 15.4 0.5
C4A D:HEM501 3.1 16.0 0.5
C1C D:HEM501 3.1 16.4 0.5
C1D D:HEM502 3.1 9.4 0.5
C4D D:HEM502 3.1 9.1 0.5
C4C D:HEM502 3.1 9.3 0.5
C4A D:HEM502 3.1 9.3 0.5
C1A D:HEM502 3.2 9.1 0.5
CZ D:TYR340 3.3 13.5 1.0
CHC D:HEM502 3.3 10.2 0.5
CHD D:HEM501 3.4 15.5 0.5
CHA D:HEM501 3.4 15.2 0.5
CHC D:HEM501 3.5 17.2 0.5
CHB D:HEM501 3.5 15.8 0.5
CHB D:HEM502 3.5 9.7 0.5
CHD D:HEM502 3.5 9.3 0.5
CHA D:HEM502 3.5 9.0 0.5
CE1 D:TYR340 4.1 12.7 1.0
CE2 D:TYR340 4.1 13.0 1.0
C3C D:HEM501 4.2 16.1 0.5
C2D D:HEM501 4.2 14.8 0.5
C3B D:HEM502 4.2 10.2 0.5
C2B D:HEM502 4.2 10.3 0.5
C3D D:HEM501 4.2 14.5 0.5
C2B D:HEM501 4.2 15.7 0.5
C3B D:HEM501 4.2 17.0 0.5
C2C D:HEM501 4.3 15.8 0.5
C2C D:HEM502 4.3 9.9 0.5
C2A D:HEM501 4.3 15.0 0.5
C3A D:HEM501 4.3 14.9 0.5
NE D:ARG336 4.3 13.6 1.0
O D:HOH991 4.3 21.1 1.0
CZ D:PHE143 4.3 14.8 1.0
C3C D:HEM502 4.3 9.5 0.5
C3A D:HEM502 4.3 9.1 0.5
NE2 D:HIS57 4.3 15.8 1.0
CG2 D:VAL56 4.4 11.7 1.0
C2D D:HEM502 4.4 8.8 0.5
C3D D:HEM502 4.4 8.9 0.5
C2A D:HEM502 4.4 8.8 0.5
NH2 D:ARG336 4.4 14.9 1.0
CD2 D:HIS57 4.5 14.2 1.0
CZ D:ARG336 4.8 14.4 1.0
CE2 D:PHE143 4.9 15.3 1.0
CE1 D:PHE143 4.9 15.5 1.0

Iron binding site 8 out of 8 in 4qol

Go back to Iron Binding Sites List in 4qol
Iron binding site 8 out of 8 in the Structure of Bacillus Pumilus Catalase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe502

b:9.8
occ:0.50
 FE D:HEM502 0.0 9.8 0.5
FE D:HEM501 0.6 20.9 0.5
OH D:TYR340 1.8 15.8 1.0
ND D:HEM502 1.9 9.0 0.5
ND D:HEM501 1.9 16.1 0.5
NA D:HEM501 2.0 15.0 0.5
NA D:HEM502 2.0 9.6 0.5
NB D:HEM502 2.1 9.9 0.5
NC D:HEM502 2.1 9.9 0.5
NB D:HEM501 2.2 17.5 0.5
NC D:HEM501 2.3 15.7 0.5
CZ D:TYR340 2.8 13.5 1.0
C4D D:HEM501 2.9 15.5 0.5
C1D D:HEM501 2.9 15.5 0.5
O D:HOH993 2.9 28.2 1.0
C1D D:HEM502 2.9 9.4 0.5
C4D D:HEM502 3.0 9.1 0.5
C1A D:HEM501 3.0 15.4 0.5
C4A D:HEM501 3.0 16.0 0.5
C4B D:HEM502 3.0 10.1 0.5
C1A D:HEM502 3.1 9.1 0.5
C4A D:HEM502 3.1 9.3 0.5
C1B D:HEM501 3.1 15.9 0.5
C1B D:HEM502 3.1 10.0 0.5
C4C D:HEM502 3.1 9.3 0.5
C4C D:HEM501 3.1 16.5 0.5
C1C D:HEM502 3.1 9.9 0.5
C4B D:HEM501 3.2 16.8 0.5
C1C D:HEM501 3.3 16.4 0.5
CHA D:HEM501 3.3 15.2 0.5
CHA D:HEM502 3.4 9.0 0.5
CHB D:HEM501 3.4 15.8 0.5
CHD D:HEM501 3.4 15.5 0.5
CHD D:HEM502 3.4 9.3 0.5
CHC D:HEM502 3.5 10.2 0.5
CHB D:HEM502 3.5 9.7 0.5
CE2 D:TYR340 3.6 13.0 1.0
CE1 D:TYR340 3.6 12.7 1.0
CHC D:HEM501 3.6 17.2 0.5
NE D:ARG336 4.0 13.6 1.0
NH2 D:ARG336 4.1 14.9 1.0
C2A D:HEM501 4.1 15.0 0.5
C2D D:HEM501 4.2 14.8 0.5
C3A D:HEM501 4.2 14.9 0.5
C3D D:HEM501 4.2 14.5 0.5
C3A D:HEM502 4.2 9.1 0.5
C2D D:HEM502 4.2 8.8 0.5
C3D D:HEM502 4.2 8.9 0.5
C3C D:HEM501 4.3 16.1 0.5
C2A D:HEM502 4.3 8.8 0.5
C2B D:HEM502 4.3 10.3 0.5
C2B D:HEM501 4.3 15.7 0.5
C3C D:HEM502 4.3 9.5 0.5
C2C D:HEM502 4.3 9.9 0.5
C3B D:HEM502 4.3 10.2 0.5
C3B D:HEM501 4.3 17.0 0.5
C2C D:HEM501 4.4 15.8 0.5
CZ D:ARG336 4.5 14.4 1.0
NE2 D:HIS57 4.7 15.8 1.0
CG2 D:VAL56 4.7 11.7 1.0
CZ D:PHE143 4.7 14.8 1.0
O D:HOH991 4.8 21.1 1.0
CD2 D:TYR340 4.8 12.9 1.0
CD2 D:HIS57 4.8 14.2 1.0
CD1 D:TYR340 4.8 12.5 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: Sun Dec 13 15:44:56 2020

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