Molybdenum in PDB 1fdi: Oxidized Form of Formate Dehydrogenase H From E. Coli Complexed with the Inhibitor Nitrite

Enzymatic activity of Oxidized Form of Formate Dehydrogenase H From E. Coli Complexed with the Inhibitor Nitrite

All present enzymatic activity of Oxidized Form of Formate Dehydrogenase H From E. Coli Complexed with the Inhibitor Nitrite:
1.2.1.2;

Protein crystallography data

The structure of Oxidized Form of Formate Dehydrogenase H From E. Coli Complexed with the Inhibitor Nitrite, PDB code: 1fdi was solved by P.D.Sun, J.C.Boyington, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	6.00 / 2.90
*Space group*	P 4₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	146.800, 146.800, 81.800, 90.00, 90.00, 90.00
*R / R_free (%)*	19.2 / 28.4

Other elements in 1fdi:

The structure of Oxidized Form of Formate Dehydrogenase H From E. Coli Complexed with the Inhibitor Nitrite also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Oxidized Form of Formate Dehydrogenase H From E. Coli Complexed with the Inhibitor Nitrite (pdb code 1fdi). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total only one binding site of Molybdenum was determined in the Oxidized Form of Formate Dehydrogenase H From E. Coli Complexed with the Inhibitor Nitrite, PDB code: 1fdi:

Molybdenum binding site 1 out of 1 in 1fdi

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Molybdenum Binding Sites List in 1fdi

Molybdenum binding site 1 out of 1 in the Oxidized Form of Formate Dehydrogenase H From E. Coli Complexed with the Inhibitor Nitrite

Mono view

Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Oxidized Form of Formate Dehydrogenase H From E. Coli Complexed with the Inhibitor Nitrite within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mo803 b:30.3 occ:1.00	S13	A:MGD801	2.2	27.2	1.0
	S12	A:MGD802	2.5	32.0	1.0
	S13	A:MGD802	2.5	29.2	1.0
	S12	A:MGD801	2.5	30.9	1.0
	O1	A:NO2804	2.6	28.6	1.0
	SE	A:SEC140	2.7	36.5	1.0
	CB	A:SEC140	3.3	33.5	1.0
	C13	A:MGD801	3.4	29.7	1.0
	C13	A:MGD802	3.5	28.8	1.0
	C12	A:MGD802	3.5	29.4	1.0
	C12	A:MGD801	3.5	29.7	1.0
	N	A:NO2804	3.6	30.7	1.0
	CG	A:GLN335	4.1	13.0	1.0
	CA	A:GLY334	4.1	15.0	1.0
	N	A:GLN335	4.2	13.7	1.0
	O2	A:NO2804	4.4	26.6	1.0
	CE	A:MET297	4.5	16.4	1.0
	CA	A:SEC140	4.6	32.6	1.0
	NH1	A:ARG581	4.6	43.6	1.0
	C	A:GLY334	4.7	14.1	1.0
	N	A:GLY334	4.7	17.1	1.0
	C14	A:MGD801	4.8	29.8	1.0
	C14	A:MGD802	4.9	28.4	1.0
	C11	A:MGD802	4.9	28.1	1.0
	C11	A:MGD801	4.9	29.5	1.0
	CD	A:GLN335	5.0	15.6	1.0

Reference:

J.C.Boyington, V.N.Gladyshev, S.V.Khangulov, T.C.Stadtman, P.D.Sun. Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and An FE4S4 Cluster. Science V. 275 1305 1997.
ISSN: ISSN 0036-8075
PubMed: 9036855
DOI: 10.1126/SCIENCE.275.5304.1305

Page generated: Sun Aug 17 02:51:48 2025

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