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Iron in PDB 4b7g: Structure of A Bacterial Catalase

Enzymatic activity of Structure of A Bacterial Catalase

All present enzymatic activity of Structure of A Bacterial Catalase:
1.11.1.6;

Protein crystallography data

The structure of Structure of A Bacterial Catalase, PDB code: 4b7g was solved by A.Gumiero, M.Walsh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.802 / 1.90
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 151.751, 151.751, 157.682, 90.00, 90.00, 120.00
R / Rfree (%) 13.3 / 17.43

Other elements in 4b7g:

The structure of Structure of A Bacterial Catalase also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of A Bacterial Catalase (pdb code 4b7g). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of A Bacterial Catalase, PDB code: 4b7g:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4b7g

Go back to Iron Binding Sites List in 4b7g
Iron binding site 1 out of 4 in the Structure of A Bacterial 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 A Bacterial Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe3000

b:13.6
occ:1.00
FE A:HEM3000 0.0 13.6 1.0
OH A:TYR353 2.0 13.6 1.0
NC A:HEM3000 2.0 18.5 1.0
NB A:HEM3000 2.0 11.8 1.0
NA A:HEM3000 2.1 12.5 1.0
ND A:HEM3000 2.1 12.7 1.0
O A:HOH2120 2.5 30.0 1.0
CZ A:TYR353 3.0 10.7 1.0
C4C A:HEM3000 3.0 16.0 1.0
C1C A:HEM3000 3.0 16.1 1.0
C1D A:HEM3000 3.1 14.2 1.0
C1B A:HEM3000 3.1 11.5 1.0
C4A A:HEM3000 3.1 14.5 1.0
C4B A:HEM3000 3.1 15.0 1.0
C1A A:HEM3000 3.1 13.6 1.0
C4D A:HEM3000 3.1 14.5 1.0
CHD A:HEM3000 3.4 13.8 1.0
CHB A:HEM3000 3.4 12.5 1.0
CHC A:HEM3000 3.4 15.6 1.0
CHA A:HEM3000 3.5 11.5 1.0
CE2 A:TYR353 3.7 13.3 1.0
CE1 A:TYR353 3.8 10.7 1.0
NE A:ARG349 3.9 9.5 1.0
O A:HOH2119 4.2 26.3 1.0
C3C A:HEM3000 4.2 10.9 1.0
C2C A:HEM3000 4.2 16.2 1.0
NH2 A:ARG349 4.2 11.7 1.0
C3A A:HEM3000 4.3 14.2 1.0
C2B A:HEM3000 4.3 13.4 1.0
C3B A:HEM3000 4.3 11.4 1.0
C2A A:HEM3000 4.3 11.4 1.0
C2D A:HEM3000 4.3 12.2 1.0
C3D A:HEM3000 4.3 14.3 1.0
CZ A:PHE156 4.5 14.0 1.0
NE2 A:HIS71 4.5 14.8 1.0
CZ A:ARG349 4.5 14.6 1.0
CD2 A:HIS71 4.7 10.4 1.0
CD A:ARG349 4.9 11.2 1.0
CD2 A:TYR353 5.0 11.9 1.0

Iron binding site 2 out of 4 in 4b7g

Go back to Iron Binding Sites List in 4b7g
Iron binding site 2 out of 4 in the Structure of A Bacterial 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 A Bacterial Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe3001

b:15.4
occ:1.00
FE B:HEM3001 0.0 15.4 1.0
OH B:TYR353 1.9 16.7 1.0
NB B:HEM3001 2.0 14.8 1.0
NA B:HEM3001 2.0 12.3 1.0
ND B:HEM3001 2.1 13.5 1.0
NC B:HEM3001 2.1 16.2 1.0
O B:HOH2073 2.5 30.0 1.0
CZ B:TYR353 2.9 12.4 1.0
C4A B:HEM3001 3.0 15.4 1.0
C1B B:HEM3001 3.0 15.1 1.0
C1D B:HEM3001 3.1 13.0 1.0
C1A B:HEM3001 3.1 14.0 1.0
C4C B:HEM3001 3.1 16.7 1.0
C4B B:HEM3001 3.1 18.2 1.0
C4D B:HEM3001 3.1 18.0 1.0
C1C B:HEM3001 3.1 15.2 1.0
CHB B:HEM3001 3.4 14.2 1.0
CHD B:HEM3001 3.4 14.7 1.0
CHA B:HEM3001 3.4 13.1 1.0
CHC B:HEM3001 3.5 15.0 1.0
CE2 B:TYR353 3.7 15.1 1.0
CE1 B:TYR353 3.7 12.4 1.0
NE B:ARG349 3.9 12.9 1.0
NH2 B:ARG349 4.2 13.0 1.0
C3A B:HEM3001 4.2 16.3 1.0
C2A B:HEM3001 4.3 10.9 1.0
C2B B:HEM3001 4.3 13.8 1.0
C3C B:HEM3001 4.3 17.4 1.0
O B:HOH2074 4.3 23.0 1.0
C3B B:HEM3001 4.3 16.2 1.0
C2D B:HEM3001 4.3 13.4 1.0
C2C B:HEM3001 4.3 13.8 1.0
C3D B:HEM3001 4.3 13.4 1.0
CZ B:ARG349 4.4 12.4 1.0
CZ B:PHE156 4.5 14.9 1.0
NE2 B:HIS71 4.7 15.9 1.0
CD2 B:HIS71 4.8 11.7 1.0
CD B:ARG349 4.8 14.1 1.0
CD2 B:TYR353 4.9 12.6 1.0
CD1 B:TYR353 5.0 13.6 1.0
CD B:PRO70 5.0 13.7 1.0

Iron binding site 3 out of 4 in 4b7g

Go back to Iron Binding Sites List in 4b7g
Iron binding site 3 out of 4 in the Structure of A Bacterial 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 A Bacterial Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe3002

b:14.0
occ:1.00
FE C:HEM3002 0.0 14.0 1.0
OH C:TYR353 2.0 15.0 1.0
NA C:HEM3002 2.0 14.1 1.0
ND C:HEM3002 2.0 11.6 1.0
NB C:HEM3002 2.0 12.2 1.0
NC C:HEM3002 2.1 17.2 1.0
O C:HOH2089 2.2 30.0 1.0
CZ C:TYR353 3.0 14.1 1.0
C1D C:HEM3002 3.0 15.9 1.0
C4C C:HEM3002 3.0 15.2 1.0
C4A C:HEM3002 3.0 11.7 1.0
C1A C:HEM3002 3.0 12.0 1.0
C1B C:HEM3002 3.0 16.1 1.0
C4D C:HEM3002 3.1 14.7 1.0
C4B C:HEM3002 3.1 14.8 1.0
C1C C:HEM3002 3.1 14.6 1.0
CHD C:HEM3002 3.4 10.8 1.0
CHB C:HEM3002 3.4 11.1 1.0
CHA C:HEM3002 3.4 13.6 1.0
CHC C:HEM3002 3.5 15.0 1.0
CE2 C:TYR353 3.7 11.5 1.0
CE1 C:TYR353 3.8 14.2 1.0
NE C:ARG349 4.0 11.4 1.0
C3A C:HEM3002 4.2 12.1 1.0
C2A C:HEM3002 4.2 10.7 1.0
C3C C:HEM3002 4.2 17.1 1.0
C2D C:HEM3002 4.3 14.3 1.0
NH2 C:ARG349 4.3 13.7 1.0
C3D C:HEM3002 4.3 13.9 1.0
C2B C:HEM3002 4.3 14.8 1.0
C2C C:HEM3002 4.3 16.8 1.0
O C:HOH2090 4.3 24.0 1.0
C3B C:HEM3002 4.3 13.2 1.0
CZ C:PHE156 4.5 13.4 1.0
CZ C:ARG349 4.5 15.0 1.0
NE2 C:HIS71 4.5 14.7 1.0
CD2 C:HIS71 4.7 10.8 1.0
CD C:ARG349 4.9 12.5 1.0
CD2 C:TYR353 5.0 10.4 1.0

Iron binding site 4 out of 4 in 4b7g

Go back to Iron Binding Sites List in 4b7g
Iron binding site 4 out of 4 in the Structure of A Bacterial 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 A Bacterial Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe3003

b:13.6
occ:1.00
FE D:HEM3003 0.0 13.6 1.0
OH D:TYR353 1.9 14.1 1.0
ND D:HEM3003 2.0 10.5 1.0
NC D:HEM3003 2.1 15.6 1.0
NA D:HEM3003 2.1 12.6 1.0
NB D:HEM3003 2.1 11.6 1.0
O D:HOH2064 2.3 30.0 1.0
CZ D:TYR353 2.9 16.3 1.0
C1D D:HEM3003 3.0 14.8 1.0
C4C D:HEM3003 3.0 17.4 1.0
C4A D:HEM3003 3.0 7.8 1.0
C4D D:HEM3003 3.1 14.4 1.0
C1B D:HEM3003 3.1 12.9 1.0
C1A D:HEM3003 3.1 14.0 1.0
C4B D:HEM3003 3.1 14.2 1.0
C1C D:HEM3003 3.1 17.3 1.0
CHD D:HEM3003 3.4 15.2 1.0
CHB D:HEM3003 3.4 11.8 1.0
CHA D:HEM3003 3.5 13.3 1.0
CHC D:HEM3003 3.5 15.8 1.0
CE2 D:TYR353 3.7 11.5 1.0
CE1 D:TYR353 3.8 9.9 1.0
NE D:ARG349 3.9 10.3 1.0
C3C D:HEM3003 4.2 17.2 1.0
NH2 D:ARG349 4.2 12.2 1.0
C2D D:HEM3003 4.2 12.8 1.0
C3A D:HEM3003 4.2 11.4 1.0
C2A D:HEM3003 4.3 11.5 1.0
C3D D:HEM3003 4.3 15.2 1.0
C2C D:HEM3003 4.3 16.6 1.0
C2B D:HEM3003 4.3 16.9 1.0
C3B D:HEM3003 4.3 15.8 1.0
CZ D:PHE156 4.5 14.1 1.0
O D:HOH2063 4.5 21.0 1.0
CZ D:ARG349 4.5 14.7 1.0
NE2 D:HIS71 4.6 14.6 1.0
CD2 D:HIS71 4.8 12.6 1.0
CD D:ARG349 4.9 11.2 1.0
CD2 D:TYR353 4.9 12.6 1.0
CD1 D:TYR353 5.0 11.7 1.0

Reference:

M.Candelaresi, A.Gumiero, K.Adamczyk, K.Robb, C.Bellota-Anton, V.Sangal, J.Munnoch, G.M.Greetham, M.Towrie, P.A.Hoskisson, A.W.Parker, N.P.Tucker, M.A.Walsh, N.T.Hunt. A Structural and Dynamic Investigation of the Inhibition of Catalase By Nitric Oxide. Org.Biomol.Chem. V. 11 7778 2013.
ISSN: ISSN 1477-0520
PubMed: 24121528
DOI: 10.1039/C3OB41977K
Page generated: Sun Dec 13 15:28:48 2020

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