Cobalt in PDB 4req: Methylmalonyl-Coa Mutase Substrate Complex

All present enzymatic activity of Methylmalonyl-Coa Mutase Substrate Complex:
5.4.99.2;

The structure of Methylmalonyl-Coa Mutase Substrate Complex, PDB code: 4req 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 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	120.130, 160.900, 88.500, 90.00, 104.64, 90.00
R / Rfree (%)	22.2 / 27.7

The binding sites of Cobalt atom in the Methylmalonyl-Coa Mutase Substrate Complex (pdb code 4req). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Methylmalonyl-Coa Mutase Substrate Complex, PDB code: 4req:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Methylmalonyl-Coa Mutase Substrate Complex


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 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Co800 b:20.6 occ:1.00 CO A:B12800 0.0 20.6 1.0 N21 A:B12800 1.7 14.3 1.0 N23 A:B12800 1.8 16.0 1.0 N24 A:B12800 1.8 14.9 1.0 N22 A:B12800 1.9 18.9 1.0 NE2 A:HIS610 2.5 22.4 1.0 C4 A:B12800 2.7 18.1 1.0 C1 A:B12800 2.8 17.0 1.0 C19 A:B12800 2.8 11.4 1.0 C11 A:B12800 2.8 16.5 1.0 C16 A:B12800 2.9 14.8 1.0 C14 A:B12800 2.9 18.1 1.0 C9 A:B12800 2.9 18.1 1.0 C6 A:B12800 2.9 17.5 1.0 C5 A:B12800 3.2 20.8 1.0 C10 A:B12800 3.3 15.9 1.0 CD2 A:HIS610 3.3 21.7 1.0 C15 A:B12800 3.4 17.3 1.0 CE1 A:HIS610 3.5 21.4 1.0 C20 A:B12800 3.5 21.5 1.0 C2 A:B12800 4.0 17.5 1.0 C3 A:B12800 4.0 18.8 1.0 C18 A:B12800 4.1 16.1 1.0 C12 A:B12800 4.2 17.2 1.0 C13 A:B12800 4.2 18.2 1.0 C17 A:B12800 4.2 18.2 1.0 C8 A:B12800 4.2 17.6 1.0 C7 A:B12800 4.3 20.4 1.0 C26 A:B12800 4.4 15.8 1.0 CG A:HIS610 4.5 23.5 1.0 ND1 A:HIS610 4.5 24.9 1.0 C42 A:B12800 4.5 20.9 1.0 C5' A:5AD803 4.6 35.0 0.5 C54 A:B12800 4.6 14.3 1.0 C46 A:B12800 4.7 13.6 1.0 C48 A:B12800 4.7 16.8 1.0 O A:HOH1165 4.7 44.4 1.0 C35 A:B12800 4.8 23.4 1.0 C53 A:B12800 4.9 21.2 1.0 C3' A:5AD803 5.0 34.8 0.5

Cobalt binding site 2 out of 2 in the Methylmalonyl-Coa Mutase Substrate Complex


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Methylmalonyl-Coa Mutase Substrate Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Co800 b:16.2 occ:1.00 CO C:B12800 0.0 16.2 1.0 N21 C:B12800 1.7 10.6 1.0 N24 C:B12800 1.8 11.3 1.0 N23 C:B12800 1.9 16.2 1.0 N22 C:B12800 1.9 15.1 1.0 NE2 C:HIS610 2.4 15.2 1.0 C1 C:B12800 2.7 15.8 1.0 C19 C:B12800 2.8 11.5 1.0 C9 C:B12800 2.8 13.7 1.0 C4 C:B12800 2.8 14.6 1.0 C11 C:B12800 2.9 15.1 1.0 C16 C:B12800 2.9 12.6 1.0 C14 C:B12800 2.9 15.2 1.0 C6 C:B12800 3.0 14.6 1.0 C10 C:B12800 3.2 13.3 1.0 CD2 C:HIS610 3.3 11.6 1.0 C5 C:B12800 3.3 16.6 1.0 C20 C:B12800 3.4 18.6 1.0 C15 C:B12800 3.4 13.4 1.0 CE1 C:HIS610 3.4 15.8 1.0 C2 C:B12800 4.0 15.0 1.0 C18 C:B12800 4.1 15.1 1.0 C3 C:B12800 4.1 14.9 1.0 C17 C:B12800 4.2 14.2 1.0 C13 C:B12800 4.2 16.8 1.0 C12 C:B12800 4.2 16.3 1.0 C8 C:B12800 4.2 15.9 1.0 C7 C:B12800 4.3 16.4 1.0 C26 C:B12800 4.4 11.4 1.0 CG C:HIS610 4.5 15.8 1.0 ND1 C:HIS610 4.5 21.6 1.0 O C:HOH1162 4.5 33.4 1.0 C5' C:5AD803 4.5 37.9 0.5 C42 C:B12800 4.6 18.2 1.0 C54 C:B12800 4.6 12.7 1.0 C48 C:B12800 4.8 18.1 1.0 C46 C:B12800 4.8 11.4 1.0 C35 C:B12800 4.9 18.4 1.0 C3' C:5AD803 4.9 37.9 0.5 C53 C:B12800 4.9 17.2 1.0 O3' C:5AD803 4.9 33.2 0.5

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