Cobalt in PDB 2req: Methylmalonyl-Coa Mutase, Non-Productive Coa Complex, in Open Conformation Representing Substrate-Free State

All present enzymatic activity of Methylmalonyl-Coa Mutase, Non-Productive Coa Complex, in Open Conformation Representing Substrate-Free State:
5.4.99.2;

The structure of Methylmalonyl-Coa Mutase, Non-Productive Coa Complex, in Open Conformation Representing Substrate-Free State, PDB code: 2req 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 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	104.950, 162.060, 104.200, 90.00, 108.75, 90.00
R / Rfree (%)	25.9 / 32.5

The binding sites of Cobalt atom in the Methylmalonyl-Coa Mutase, Non-Productive Coa Complex, in Open Conformation Representing Substrate-Free State (pdb code 2req). 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, Non-Productive Coa Complex, in Open Conformation Representing Substrate-Free State, PDB code: 2req:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Methylmalonyl-Coa Mutase, Non-Productive Coa Complex, in Open Conformation Representing Substrate-Free State


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, Non-Productive Coa Complex, in Open Conformation Representing Substrate-Free State within 5.0Å range: probe atom residue distance (Å) B Occ A:Co800 b:25.9 occ:1.00 CO A:B12800 0.0 25.9 1.0 N21 A:B12800 1.8 27.8 1.0 N24 A:B12800 1.9 21.0 1.0 N23 A:B12800 1.9 25.7 1.0 N22 A:B12800 1.9 26.9 1.0 NE2 A:HIS610 2.7 28.6 1.0 C4 A:B12800 2.8 30.4 1.0 C1 A:B12800 2.8 27.9 1.0 C19 A:B12800 2.9 23.7 1.0 C11 A:B12800 2.9 22.2 1.0 C9 A:B12800 2.9 28.9 1.0 C16 A:B12800 2.9 25.7 1.0 C6 A:B12800 2.9 29.4 1.0 C14 A:B12800 2.9 23.8 1.0 C10 A:B12800 3.2 27.4 1.0 C5 A:B12800 3.3 30.5 1.0 C15 A:B12800 3.4 27.0 1.0 C20 A:B12800 3.4 25.7 1.0 CD2 A:HIS610 3.5 31.1 1.0 CE1 A:HIS610 3.7 27.3 1.0 C2 A:B12800 4.0 29.2 1.0 C3 A:B12800 4.1 30.6 1.0 C18 A:B12800 4.1 26.0 1.0 C12 A:B12800 4.2 25.6 1.0 C17 A:B12800 4.2 27.6 1.0 C8 A:B12800 4.2 31.0 1.0 C13 A:B12800 4.2 24.5 1.0 C7 A:B12800 4.3 33.0 1.0 C26 A:B12800 4.5 31.2 1.0 C46 A:B12800 4.6 15.0 1.0 CG A:HIS610 4.7 27.5 1.0 ND1 A:HIS610 4.8 25.4 1.0 C41 A:B12800 4.8 35.8 1.0 C54 A:B12800 4.8 25.1 1.0 C37 A:B12800 4.8 37.8 1.0 C35 A:B12800 4.8 24.7 1.0 C53 A:B12800 4.9 26.9 1.0

Cobalt binding site 2 out of 2 in the Methylmalonyl-Coa Mutase, Non-Productive Coa Complex, in Open Conformation Representing Substrate-Free State


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, Non-Productive Coa Complex, in Open Conformation Representing Substrate-Free State within 5.0Å range: probe atom residue distance (Å) B Occ C:Co800 b:21.8 occ:1.00 CO C:B12800 0.0 21.8 1.0 N24 C:B12800 1.7 17.3 1.0 N23 C:B12800 1.7 12.3 1.0 N21 C:B12800 1.8 18.4 1.0 N22 C:B12800 1.9 21.0 1.0 C19 C:B12800 2.7 17.3 1.0 C14 C:B12800 2.8 17.3 1.0 C16 C:B12800 2.8 16.1 1.0 NE2 C:HIS610 2.8 24.3 1.0 C1 C:B12800 2.8 19.7 1.0 C11 C:B12800 2.8 16.0 1.0 C4 C:B12800 2.9 20.1 1.0 C6 C:B12800 3.0 26.1 1.0 C9 C:B12800 3.0 20.1 1.0 C15 C:B12800 3.2 18.3 1.0 C10 C:B12800 3.3 21.2 1.0 C5 C:B12800 3.4 24.2 1.0 C20 C:B12800 3.4 22.1 1.0 CD2 C:HIS610 3.5 21.2 1.0 CE1 C:HIS610 3.8 24.0 1.0 C18 C:B12800 4.0 20.7 1.0 C17 C:B12800 4.1 19.8 1.0 C13 C:B12800 4.1 19.0 1.0 C2 C:B12800 4.1 22.5 1.0 C12 C:B12800 4.1 21.3 1.0 C3 C:B12800 4.1 21.4 1.0 C8 C:B12800 4.3 24.8 1.0 C7 C:B12800 4.3 29.5 1.0 C26 C:B12800 4.5 26.3 1.0 C54 C:B12800 4.7 14.2 1.0 C46 C:B12800 4.7 9.2 1.0 CG C:HIS610 4.7 24.1 1.0 C53 C:B12800 4.7 22.0 1.0 C48 C:B12800 4.7 18.0 1.0 ND1 C:HIS610 4.8 25.8 1.0 C35 C:B12800 4.9 25.2 1.0 C37 C:B12800 4.9 31.2 1.0 C41 C:B12800 5.0 27.4 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