Magnesium in PDB 6x5k: Crystal Structure of Codh/Acs with Carbon Monoxide Bound to the A- Cluster

Enzymatic activity of Crystal Structure of Codh/Acs with Carbon Monoxide Bound to the A- Cluster

All present enzymatic activity of Crystal Structure of Codh/Acs with Carbon Monoxide Bound to the A- Cluster:
1.2.7.4; 2.3.1.169;

Protein crystallography data

The structure of Crystal Structure of Codh/Acs with Carbon Monoxide Bound to the A- Cluster, PDB code: 6x5k was solved by S.E.Cohen, E.C.Wittenborn, R.Hendrickson, C.L.Drennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	49.63 / 2.47
*Space group*	P 1
*Cell size a, b, c (Å), α, β, γ (°)*	99.729, 137.383, 141.867, 101.82, 109.08, 103.66
*R / R_free (%)*	20.3 / 23.4

Other elements in 6x5k:

The structure of Crystal Structure of Codh/Acs with Carbon Monoxide Bound to the A- Cluster also contains other interesting chemical elements:

Nickel	(Ni)	12 atoms
Iron	(Fe)	56 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Codh/Acs with Carbon Monoxide Bound to the A- Cluster (pdb code 6x5k). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Codh/Acs with Carbon Monoxide Bound to the A- Cluster, PDB code: 6x5k:

Magnesium binding site 1 out of 1 in 6x5k

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Magnesium Binding Sites List in 6x5k

Magnesium binding site 1 out of 1 in the Crystal Structure of Codh/Acs with Carbon Monoxide Bound to the A- Cluster

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Codh/Acs with Carbon Monoxide Bound to the A- Cluster within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
N:Mg805 b:43.8 occ:1.00	O	N:LEU417	2.3	44.8	1.0
	O	N:ASN412	2.4	38.0	1.0
	O	N:PHE328	2.5	38.0	1.0
	O	N:HOH962	2.5	34.8	1.0
	O	N:GLY414	2.6	41.8	1.0
	OE1	N:GLU331	2.8	52.5	1.0
	C	N:ASN412	3.3	38.4	1.0
	C	N:LEU417	3.5	42.7	1.0
	C	N:PHE328	3.5	41.1	1.0
	CA	N:ASN412	3.7	40.5	1.0
	C	N:GLY414	3.7	38.1	1.0
	CB	N:GLU331	3.8	54.1	1.0
	CB	N:PHE328	3.9	35.7	1.0
	CD	N:GLU331	3.9	54.0	1.0
	N	N:LEU417	4.0	38.5	1.0
	CA	N:LEU417	4.3	36.7	1.0
	N	N:GLY414	4.3	37.6	1.0
	CA	N:PHE328	4.3	40.8	1.0
	CB	N:ASN412	4.4	38.6	1.0
	CG	N:GLU331	4.4	53.2	1.0
	N	N:GLY416	4.4	33.3	1.0
	N	N:GLU329	4.4	43.3	1.0
	N	N:TYR413	4.5	36.2	1.0
	N	N:TRP418	4.5	41.5	1.0
	OD1	N:ASN412	4.5	35.0	1.0
	O	N:ILE411	4.6	45.6	1.0
	CA	N:GLU329	4.6	46.6	1.0
	N	N:GLU415	4.6	36.2	1.0
	CA	N:GLY414	4.6	37.6	1.0
	CA	N:GLU415	4.6	36.0	1.0
	C	N:TYR413	4.6	38.4	1.0
	CA	N:TRP418	4.7	39.8	1.0
	O	N:GLU329	4.7	49.9	1.0
	CB	N:LEU417	4.7	30.8	1.0
	C	N:GLU329	4.9	47.1	1.0
	OE2	N:GLU331	4.9	56.1	1.0
	C	N:GLY416	4.9	39.0	1.0
	N	N:GLU331	4.9	53.2	1.0
	CA	N:TYR413	4.9	35.5	1.0
	CA	N:GLU331	4.9	53.4	1.0
	CG	N:ASN412	4.9	36.4	1.0
	C	N:GLU415	4.9	34.2	1.0
	N	N:ASN412	4.9	43.1	1.0

Reference:

S.E.Cohen, M.Can, E.C.Wittenborn, R.A.Hendrickson, S.W.Ragsdale, C.L.Drennan. Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase Acs Catalysis V. 10 9741 2020.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.0C03033

Page generated: Tue Oct 1 23:26:36 2024

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