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Cobalt in PDB 9fw4: Crystal Structure of Heme-Oxygenase Mutant H20C From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III))

Enzymatic activity of Crystal Structure of Heme-Oxygenase Mutant H20C From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III))

All present enzymatic activity of Crystal Structure of Heme-Oxygenase Mutant H20C From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III)):
1.14.14.18;

Protein crystallography data

The structure of Crystal Structure of Heme-Oxygenase Mutant H20C From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III)), PDB code: 9fw4 was solved by R.J.Labidi, B.Faivre, P.Carpentier, J.Perard, P.Gotico, Y.Li, M.Atta, M.Fontecave, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.16 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 43.744, 69.331, 63.177, 90, 109.62, 90
R / Rfree (%) 22.7 / 28.4

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Heme-Oxygenase Mutant H20C From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III)) (pdb code 9fw4). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Crystal Structure of Heme-Oxygenase Mutant H20C From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III)), PDB code: 9fw4:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 9fw4

Go back to Cobalt Binding Sites List in 9fw4
Cobalt binding site 1 out of 2 in the Crystal Structure of Heme-Oxygenase Mutant H20C From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III))


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Heme-Oxygenase Mutant H20C From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III)) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co901

b:35.1
occ:1.00
CO A:COH901 0.0 35.1 1.0
NA A:COH901 1.9 35.1 1.0
NC A:COH901 1.9 36.5 1.0
NB A:COH901 1.9 35.9 1.0
ND A:COH901 1.9 36.4 1.0
C4C A:COH901 3.0 37.2 1.0
C4B A:COH901 3.0 36.1 1.0
C4A A:COH901 3.0 34.9 1.0
C1A A:COH901 3.0 35.4 1.0
C1D A:COH901 3.0 36.8 1.0
C4D A:COH901 3.0 36.4 1.0
C1B A:COH901 3.0 35.3 1.0
C1C A:COH901 3.0 37.1 1.0
O A:HOH1006 3.2 38.2 1.0
CHA A:COH901 3.4 36.1 1.0
CHB A:COH901 3.4 35.0 1.0
CHD A:COH901 3.4 37.2 1.0
CHC A:COH901 3.4 36.8 1.0
SG A:CYS20 3.9 40.0 1.0
N A:GLY139 4.2 36.0 1.0
CA A:GLY139 4.3 36.2 1.0
C3C A:COH901 4.3 37.4 1.0
C3B A:COH901 4.3 35.8 1.0
C3A A:COH901 4.3 34.7 1.0
C2A A:COH901 4.3 35.3 1.0
C2D A:COH901 4.3 37.7 1.0
C3D A:COH901 4.3 37.2 1.0
C2B A:COH901 4.4 35.4 1.0
C2C A:COH901 4.4 37.9 1.0
CA A:GLY135 4.4 34.1 1.0
OE2 A:GLU24 4.7 38.5 1.0
O A:GLY135 4.8 34.8 1.0
CB A:SER138 4.9 35.4 1.0

Cobalt binding site 2 out of 2 in 9fw4

Go back to Cobalt Binding Sites List in 9fw4
Cobalt binding site 2 out of 2 in the Crystal Structure of Heme-Oxygenase Mutant H20C From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III))


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Crystal Structure of Heme-Oxygenase Mutant H20C From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III)) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co901

b:43.1
occ:1.00
CO B:COH901 0.0 43.1 1.0
NB B:COH901 1.9 43.3 1.0
NA B:COH901 1.9 42.8 1.0
ND B:COH901 1.9 43.1 1.0
NC B:COH901 1.9 43.0 1.0
C4B B:COH901 3.0 43.3 1.0
C4C B:COH901 3.0 43.0 1.0
C4D B:COH901 3.0 42.9 1.0
C4A B:COH901 3.0 42.1 1.0
C1A B:COH901 3.0 42.8 1.0
C1D B:COH901 3.0 42.7 1.0
C1B B:COH901 3.0 42.7 1.0
C1C B:COH901 3.0 43.2 1.0
CHA B:COH901 3.4 42.8 1.0
CHC B:COH901 3.4 43.5 1.0
CHB B:COH901 3.4 42.4 1.0
CHD B:COH901 3.4 42.6 1.0
SG B:CYS20 4.1 48.8 1.0
N B:GLY139 4.3 41.6 1.0
C3B B:COH901 4.3 42.7 1.0
C3C B:COH901 4.3 43.4 1.0
C3A B:COH901 4.3 42.6 1.0
C3D B:COH901 4.3 42.2 1.0
C2A B:COH901 4.3 42.6 1.0
C2D B:COH901 4.3 42.5 1.0
C2B B:COH901 4.3 42.8 1.0
C2C B:COH901 4.4 43.4 1.0
CA B:GLY139 4.4 41.3 1.0
CA B:GLY135 4.6 41.1 1.0
O B:GLY135 5.0 40.7 1.0
CB B:SER138 5.0 41.8 1.0

Reference:

R.J.Labidi, B.Faivre, P.Carpentier, J.Perard, P.Gotico, Y.Li, M.Atta, M.Fontecave. Light-Activated Artificial Co 2 -Reductase: Structure and Activity. J.Am.Chem.Soc. 2024.
ISSN: ESSN 1520-5126
PubMed: 39352411
DOI: 10.1021/JACS.4C08927
Page generated: Sun Jul 13 22:15:01 2025

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