Cobalt in PDB 3req: Methylmalonyl-Coa Mutase, Substrate-Free State (Poor Quality Structure)

All present enzymatic activity of Methylmalonyl-Coa Mutase, Substrate-Free State (Poor Quality Structure):
5.4.99.2;

The structure of Methylmalonyl-Coa Mutase, Substrate-Free State (Poor Quality Structure), PDB code: 3req was solved by P.R.Evans, F.Mancia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.70
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.910, 110.910, 257.740, 90.00, 90.00, 90.00
R / Rfree (%)	31.3 / 39.3

The binding sites of Cobalt atom in the Methylmalonyl-Coa Mutase, Substrate-Free State (Poor Quality Structure) (pdb code 3req). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Methylmalonyl-Coa Mutase, Substrate-Free State (Poor Quality Structure), PDB code: 3req:

Cobalt binding site 1 out of 1 in the Methylmalonyl-Coa Mutase, Substrate-Free State (Poor Quality Structure)


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Methylmalonyl-Coa Mutase, Substrate-Free State (Poor Quality Structure) within 5.0Å range: probe atom residue distance (Å) B Occ A:Co800 b:36.7 occ:1.00 CO A:B12800 0.0 36.7 1.0 N23 A:B12800 1.7 44.5 1.0 N21 A:B12800 1.9 51.6 1.0 N24 A:B12800 2.0 44.8 1.0 N22 A:B12800 2.0 42.5 1.0 C5' A:ADN801 2.0 56.8 1.0 NE2 A:HIS610 2.5 54.9 1.0 C14 A:B12800 2.6 48.2 1.0 C11 A:B12800 2.8 33.5 1.0 C16 A:B12800 2.9 45.0 1.0 C9 A:B12800 2.9 39.0 1.0 C1 A:B12800 2.9 49.3 1.0 C4 A:B12800 2.9 50.0 1.0 C19 A:B12800 3.0 48.7 1.0 C6 A:B12800 3.1 40.3 1.0 C15 A:B12800 3.1 45.6 1.0 C10 A:B12800 3.2 38.6 1.0 C4' A:ADN801 3.3 75.9 1.0 CD2 A:HIS610 3.3 58.8 1.0 C5 A:B12800 3.4 46.1 1.0 C20 A:B12800 3.5 50.9 1.0 CE1 A:HIS610 3.6 60.8 1.0 C13 A:B12800 3.9 45.5 1.0 C12 A:B12800 4.0 37.0 1.0 C18 A:B12800 4.1 51.4 1.0 O4' A:ADN801 4.1 80.2 1.0 C17 A:B12800 4.2 47.5 1.0 C2 A:B12800 4.2 45.8 1.0 C3 A:B12800 4.2 51.0 1.0 C8 A:B12800 4.3 32.8 1.0 C3' A:ADN801 4.4 78.3 1.0 C7 A:B12800 4.4 37.5 1.0 CG A:HIS610 4.5 59.6 1.0 C26 A:B12800 4.5 45.0 1.0 ND1 A:HIS610 4.6 61.7 1.0 C53 A:B12800 4.6 43.0 1.0 C48 A:B12800 4.6 48.0 1.0 O3' A:ADN801 4.8 83.8 1.0 C54 A:B12800 4.8 40.7 1.0 C46 A:B12800 4.9 30.7 1.0 C37 A:B12800 4.9 40.4 1.0 C35 A:B12800 4.9 55.5 1.0

F.Mancia, P.R.Evans. Conformational Changes on Substrate Binding to Methylmalonyl Coa Mutase and New Insights Into the Free Radical Mechanism. Structure V. 6 711 1998.
ISSN: ISSN 0969-2126
PubMed: 9655823
DOI: 10.1016/S0969-2126(98)00073-2