Cobalt in PDB 6req: Methylmalonyl-Coa Mutase, 3-Carboxypropyl-Coa Inhibitor Complex

All present enzymatic activity of Methylmalonyl-Coa Mutase, 3-Carboxypropyl-Coa Inhibitor Complex:
5.4.99.2;

The structure of Methylmalonyl-Coa Mutase, 3-Carboxypropyl-Coa Inhibitor Complex, PDB code: 6req 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 (°)	119.950, 160.460, 88.480, 90.00, 105.01, 90.00
R / Rfree (%)	20.6 / 26.3

The binding sites of Cobalt atom in the Methylmalonyl-Coa Mutase, 3-Carboxypropyl-Coa Inhibitor Complex (pdb code 6req). 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, 3-Carboxypropyl-Coa Inhibitor Complex, PDB code: 6req:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Methylmalonyl-Coa Mutase, 3-Carboxypropyl-Coa Inhibitor 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, 3-Carboxypropyl-Coa Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Co1800 b:23.0 occ:1.00 CO A:B121800 0.0 23.0 1.0 N21 A:B121800 1.7 18.0 1.0 N23 A:B121800 1.8 22.6 1.0 N22 A:B121800 1.9 21.1 1.0 N24 A:B121800 2.0 21.5 1.0 NE2 A:HIS610 2.5 23.2 1.0 C4 A:B121800 2.7 18.5 1.0 C11 A:B121800 2.8 20.9 1.0 C1 A:B121800 2.8 23.7 1.0 C6 A:B121800 2.8 16.0 1.0 C9 A:B121800 2.9 16.1 1.0 C19 A:B121800 2.9 17.5 1.0 C14 A:B121800 2.9 18.4 1.0 C16 A:B121800 2.9 16.0 1.0 C5 A:B121800 3.1 13.9 1.0 C10 A:B121800 3.3 16.2 1.0 CD2 A:HIS610 3.3 25.3 1.0 C15 A:B121800 3.4 19.1 1.0 C20 A:B121800 3.5 22.7 1.0 CE1 A:HIS610 3.6 21.8 1.0 C2 A:B121800 4.0 18.0 1.0 C3 A:B121800 4.0 16.8 1.0 C12 A:B121800 4.1 24.4 1.0 C18 A:B121800 4.2 21.4 1.0 C13 A:B121800 4.2 20.5 1.0 C7 A:B121800 4.2 22.8 1.0 C8 A:B121800 4.2 18.7 1.0 C17 A:B121800 4.2 20.1 1.0 O A:HOH3357 4.3 48.3 1.0 C26 A:B121800 4.4 17.5 1.0 O A:HOH3276 4.4 40.4 1.0 CG A:HIS610 4.5 26.9 1.0 C42 A:B121800 4.6 28.2 1.0 ND1 A:HIS610 4.6 22.1 1.0 C54 A:B121800 4.6 17.0 1.0 C35 A:B121800 4.7 21.8 1.0 C46 A:B121800 4.7 17.4 1.0 C48 A:B121800 4.7 19.0 1.0 C53 A:B121800 5.0 20.0 1.0

Cobalt binding site 2 out of 2 in the Methylmalonyl-Coa Mutase, 3-Carboxypropyl-Coa Inhibitor 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, 3-Carboxypropyl-Coa Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Co2800 b:17.5 occ:1.00 CO C:B122800 0.0 17.5 1.0 N21 C:B122800 1.8 17.0 1.0 N23 C:B122800 1.8 15.2 1.0 N24 C:B122800 1.9 13.7 1.0 N22 C:B122800 2.0 22.5 1.0 NE2 C:HIS610 2.5 21.9 1.0 C1 C:B122800 2.8 17.5 1.0 C19 C:B122800 2.8 15.8 1.0 C11 C:B122800 2.8 16.4 1.0 C4 C:B122800 2.9 17.7 1.0 C9 C:B122800 2.9 18.3 1.0 C16 C:B122800 2.9 13.1 1.0 C14 C:B122800 2.9 21.5 1.0 C6 C:B122800 3.0 16.2 1.0 C10 C:B122800 3.2 11.3 1.0 CD2 C:HIS610 3.2 21.3 1.0 C5 C:B122800 3.3 19.5 1.0 C15 C:B122800 3.4 15.2 1.0 C20 C:B122800 3.5 14.1 1.0 CE1 C:HIS610 3.5 23.7 1.0 C2 C:B122800 4.1 21.4 1.0 C18 C:B122800 4.1 20.3 1.0 C3 C:B122800 4.2 18.0 1.0 C12 C:B122800 4.2 20.4 1.0 C13 C:B122800 4.2 20.3 1.0 C17 C:B122800 4.2 21.3 1.0 O C:HOH3279 4.3 39.7 1.0 C8 C:B122800 4.3 18.6 1.0 C7 C:B122800 4.3 19.2 1.0 O C:HOH3363 4.4 40.2 1.0 C26 C:B122800 4.4 21.3 1.0 CG C:HIS610 4.5 22.0 1.0 C42 C:B122800 4.5 18.1 1.0 ND1 C:HIS610 4.6 26.4 1.0 C48 C:B122800 4.7 17.1 1.0 C54 C:B122800 4.7 12.6 1.0 C46 C:B122800 4.8 15.4 1.0 C35 C:B122800 4.8 18.7 1.0 O C:HOH3362 4.9 39.0 1.0 C53 C:B122800 4.9 14.7 1.0

F.Mancia, G.A.Smith, P.R.Evans. Crystal Structure of Substrate Complexes of Methylmalonyl-Coa Mutase. Biochemistry V. 38 7999 1999.
ISSN: ISSN 0006-2960
PubMed: 10387043
DOI: 10.1021/BI9903852