Tungsten in PDB 8j83: Crystal Structure of Formate Dehydrogenase From Methylorubrum Extorquens AM1

Enzymatic activity of Crystal Structure of Formate Dehydrogenase From Methylorubrum Extorquens AM1

All present enzymatic activity of Crystal Structure of Formate Dehydrogenase From Methylorubrum Extorquens AM1:
1.17.1.9; 1.2.1.2;

Protein crystallography data

The structure of Crystal Structure of Formate Dehydrogenase From Methylorubrum Extorquens AM1, PDB code: 8j83 was solved by A.Kobayashi, M.Taketa, K.Sowa, K.Kano, Y.Higuchi, H.Ogata, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	47.48 / 2.40
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	232.86, 73.95, 95.74, 90, 106.72, 90
*R / R_free (%)*	21.9 / 25.9

Other elements in 8j83:

The structure of Crystal Structure of Formate Dehydrogenase From Methylorubrum Extorquens AM1 also contains other interesting chemical elements:

Iron

(Fe)

20 atoms

Tungsten Binding Sites:

The binding sites of Tungsten atom in the Crystal Structure of Formate Dehydrogenase From Methylorubrum Extorquens AM1 (pdb code 8j83). This binding sites where shown within 5.0 Angstroms radius around Tungsten atom.
In total only one binding site of Tungsten was determined in the Crystal Structure of Formate Dehydrogenase From Methylorubrum Extorquens AM1, PDB code: 8j83:

Tungsten binding site 1 out of 1 in 8j83

Go back to

Tungsten Binding Sites List in 8j83

Tungsten binding site 1 out of 1 in the Crystal Structure of Formate Dehydrogenase From Methylorubrum Extorquens AM1

Mono view

Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 1 of Crystal Structure of Formate Dehydrogenase From Methylorubrum Extorquens AM1 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:W1003 b:44.5 occ:1.00	O	A:HOH1101	2.1	42.4	1.0
	S12	A:MGD1002	2.5	42.4	1.0
	S13	A:MGD1002	2.5	40.1	1.0
	S13	A:MGD1001	2.5	43.6	1.0
	S12	A:MGD1001	2.5	43.7	1.0
	SG	A:CYS436	2.6	45.6	1.0
	CB	A:CYS436	3.3	44.4	1.0
	C12	A:MGD1002	3.4	41.2	1.0
	C13	A:MGD1002	3.5	41.6	1.0
	C13	A:MGD1001	3.7	42.7	1.0
	C12	A:MGD1001	3.7	42.7	1.0
	NH2	A:ARG875	4.0	41.6	1.0
	NE2	A:HIS881	4.3	42.2	1.0
	CA	A:CYS436	4.4	45.4	1.0
	CA	A:GLY631	4.5	41.6	1.0
	N	A:GLN632	4.6	41.7	1.0
	C14	A:MGD1002	4.9	41.2	1.0
	N	A:GLY631	4.9	42.2	1.0
	C11	A:MGD1002	4.9	40.6	1.0
	CE1	A:HIS881	4.9	42.3	1.0
	C	A:GLY631	4.9	41.4	1.0
	SD	A:MET594	4.9	42.6	1.0
	O	A:CYS432	5.0	46.4	1.0

Reference:

A.Kobayashi, M.Taketa, K.Sowa, K.Kano, Y.Higuchi, H.Ogata. Structure and Function Relationship of Formate Dehydrogenases: An Overview of Recent Progress. Iucrj V. 10 544 2023.
ISSN: ESSN 2052-2525
PubMed: 37668215
DOI: 10.1107/S2052252523006437

Page generated: Sat Oct 12 15:56:55 2024

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