Cobalt in PDB 1req: Methylmalonyl-Coa Mutase

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

The structure of Methylmalonyl-Coa Mutase, PDB code: 1req 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 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	119.800, 161.300, 88.400, 90.00, 105.10, 90.00
R / Rfree (%)	22 / 27.5

The binding sites of Cobalt atom in the Methylmalonyl-Coa Mutase (pdb code 1req). 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, PDB code: 1req:
Jump to Cobalt binding site number: 1; 2;

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co800 b:29.4 occ:1.00 CO A:B12800 0.0 29.4 1.0 N21 A:B12800 1.6 17.8 1.0 N23 A:B12800 1.7 17.1 1.0 N24 A:B12800 1.9 29.6 1.0 N22 A:B12800 2.0 33.5 1.0 NE2 A:HIS610 2.5 31.1 1.0 C1 A:B12800 2.7 29.5 1.0 C4 A:B12800 2.7 28.3 1.0 C11 A:B12800 2.8 31.2 1.0 C19 A:B12800 2.8 23.7 1.0 C14 A:B12800 2.9 22.5 1.0 C16 A:B12800 2.9 23.5 1.0 C9 A:B12800 3.0 31.9 1.0 C6 A:B12800 3.0 32.4 1.0 C5 A:B12800 3.3 31.7 1.0 C10 A:B12800 3.3 36.0 1.0 CD2 A:HIS610 3.3 30.9 1.0 C20 A:B12800 3.4 23.8 1.0 C15 A:B12800 3.4 26.6 1.0 CE1 A:HIS610 3.5 36.2 1.0 C2 A:B12800 3.9 28.9 1.0 C3 A:B12800 4.0 28.6 1.0 C18 A:B12800 4.1 25.6 1.0 C12 A:B12800 4.1 29.3 1.0 C13 A:B12800 4.1 24.1 1.0 C17 A:B12800 4.2 29.7 1.0 C26 A:B12800 4.3 30.4 1.0 C7 A:B12800 4.3 35.1 1.0 C8 A:B12800 4.4 40.5 1.0 CG A:HIS610 4.5 33.4 1.0 C54 A:B12800 4.6 29.1 1.0 ND1 A:HIS610 4.6 31.5 1.0 O A:HOH1136 4.6 51.2 1.0 C46 A:B12800 4.8 29.3 1.0 C35 A:B12800 4.8 32.3 1.0 C48 A:B12800 4.9 30.0 1.0 C42 A:B12800 4.9 61.3 1.0 C53 A:B12800 4.9 24.5 1.0

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ C:Co800 b:24.5 occ:1.00 CO C:B12800 0.0 24.5 1.0 N21 C:B12800 1.6 15.2 1.0 N23 C:B12800 1.7 17.5 1.0 N24 C:B12800 1.9 22.9 1.0 N22 C:B12800 2.1 30.3 1.0 NE2 C:HIS610 2.5 30.6 1.0 C1 C:B12800 2.7 25.3 1.0 C4 C:B12800 2.7 23.0 1.0 C19 C:B12800 2.8 18.7 1.0 C14 C:B12800 2.8 24.9 1.0 C11 C:B12800 2.9 27.1 1.0 C16 C:B12800 2.9 22.6 1.0 O C:HOH1141 2.9 69.5 1.0 C9 C:B12800 3.0 20.4 1.0 C6 C:B12800 3.0 21.8 1.0 C10 C:B12800 3.3 23.9 1.0 C5 C:B12800 3.3 26.8 1.0 C15 C:B12800 3.4 21.7 1.0 C20 C:B12800 3.4 25.7 1.0 CD2 C:HIS610 3.4 31.0 1.0 CE1 C:HIS610 3.5 28.7 1.0 C2 C:B12800 4.0 26.1 1.0 C3 C:B12800 4.0 22.5 1.0 C13 C:B12800 4.1 22.2 1.0 C18 C:B12800 4.1 20.8 1.0 C12 C:B12800 4.1 25.4 1.0 C17 C:B12800 4.2 27.7 1.0 C26 C:B12800 4.4 24.4 1.0 C8 C:B12800 4.4 32.6 1.0 C7 C:B12800 4.4 26.5 1.0 ND1 C:HIS610 4.6 31.7 1.0 CG C:HIS610 4.6 27.3 1.0 C48 C:B12800 4.7 28.5 1.0 C54 C:B12800 4.7 21.5 1.0 C46 C:B12800 4.7 23.3 1.0 C35 C:B12800 4.8 28.5 1.0 C53 C:B12800 4.9 20.6 1.0 C30 C:B12800 4.9 20.5 1.0

F.Mancia, N.H.Keep, A.Nakagawa, P.F.Leadlay, S.Mcsweeney, B.Rasmussen, P.Bosecke, O.Diat, P.R.Evans. How Coenzyme B12 Radicals Are Generated: the Crystal Structure of Methylmalonyl-Coenzyme A Mutase at 2 A Resolution. Structure V. 4 339 1996.
ISSN: ISSN 0969-2126
PubMed: 8805541
DOI: 10.1016/S0969-2126(96)00037-8