Nickel in PDB 1suf: Carbon Monoxide Dehydrogenase From Carboxydothermus Hydrogenoformans- Inactive State

Enzymatic activity of Carbon Monoxide Dehydrogenase From Carboxydothermus Hydrogenoformans- Inactive State

All present enzymatic activity of Carbon Monoxide Dehydrogenase From Carboxydothermus Hydrogenoformans- Inactive State:
1.2.99.2;

Protein crystallography data

The structure of Carbon Monoxide Dehydrogenase From Carboxydothermus Hydrogenoformans- Inactive State, PDB code: 1suf was solved by H.Dobbek, V.Svetlitchnyi, J.Liss, O.Meyer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	8.00 / 1.15
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	112.614, 75.004, 71.374, 90.00, 110.97, 90.00
*R / R_free (%)*	15.2 / 19

Other elements in 1suf:

The structure of Carbon Monoxide Dehydrogenase From Carboxydothermus Hydrogenoformans- Inactive State also contains other interesting chemical elements:

Iron

(Fe)

11 atoms

Nickel Binding Sites:

The binding sites of Nickel atom in the Carbon Monoxide Dehydrogenase From Carboxydothermus Hydrogenoformans- Inactive State (pdb code 1suf). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Carbon Monoxide Dehydrogenase From Carboxydothermus Hydrogenoformans- Inactive State, PDB code: 1suf:

Nickel binding site 1 out of 1 in 1suf

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Nickel Binding Sites List in 1suf

Nickel binding site 1 out of 1 in the Carbon Monoxide Dehydrogenase From Carboxydothermus Hydrogenoformans- Inactive State

Mono view

Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Carbon Monoxide Dehydrogenase From Carboxydothermus Hydrogenoformans- Inactive State within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Ni639 b:1.6 occ:0.60	NI1	A:NFS639	0.0	1.6	0.6
	FE1	A:NFS639	2.0	7.6	0.3
	SG	A:CYS526	2.1	10.9	1.0
	S3	A:NFS639	2.2	13.3	1.0
	S5	A:NFS639	2.4	11.2	1.0
	FE3	A:NFS639	2.8	0.3	1.0
	O	A:HOH1433	2.8	27.7	1.0
	O	A:HOH1423	2.8	25.3	1.0
	O	A:HOH1636	3.0	21.4	1.0
	FE1	A:NFS639	3.1	4.3	0.6
	CB	A:CYS526	3.3	11.0	1.0
	FE4	A:NFS639	3.6	0.1	1.0
	FE2	A:NFS639	3.8	0.5	1.0
	S1	A:NFS639	4.1	11.9	1.0
	O	A:HOH736	4.3	9.9	1.0
	CA	A:GLY445	4.4	9.1	1.0
	SG	A:CYS295	4.4	13.8	1.0
	SG	A:CYS446	4.5	10.4	1.0
	CA	A:CYS526	4.6	9.7	1.0
	NZ	A:LYS563	4.8	11.3	1.0
	S4	A:NFS639	4.8	10.8	1.0
	C	A:GLY445	4.8	8.9	1.0
	N	A:CYS446	5.0	8.4	1.0
	N	A:GLY445	5.0	9.3	1.0

Reference:

H.Dobbek, V.Svetlitchnyi, J.Liss, O.Meyer. Carbon Monoxide Induced Decomposition of the Active Site [Ni-4FE-5S] Cluster of Co Dehydrogenase J.Am.Chem.Soc. V. 126 5382 2004.
ISSN: ISSN 0002-7863
PubMed: 15113209
DOI: 10.1021/JA037776V

Page generated: Wed Oct 9 16:26:08 2024

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