Cobalt in PDB 7req: Methylmalonyl-Coa Mutase, 2-Carboxypropyl-Coa Inhibitor Complex

All present enzymatic activity of Methylmalonyl-Coa Mutase, 2-Carboxypropyl-Coa Inhibitor Complex:
5.4.99.2;

The structure of Methylmalonyl-Coa Mutase, 2-Carboxypropyl-Coa Inhibitor Complex, PDB code: 7req 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 (°)	122.534, 161.398, 86.973, 90.00, 104.81, 90.00
R / Rfree (%)	18.3 / 22.9

The binding sites of Cobalt atom in the Methylmalonyl-Coa Mutase, 2-Carboxypropyl-Coa Inhibitor Complex (pdb code 7req). 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, 2-Carboxypropyl-Coa Inhibitor Complex, PDB code: 7req:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Methylmalonyl-Coa Mutase, 2-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, 2-Carboxypropyl-Coa Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Co1800 b:11.4 occ:1.00 CO A:B121800 0.0 11.4 1.0 N24 A:B121800 1.8 12.3 1.0 N23 A:B121800 1.9 10.0 1.0 N21 A:B121800 1.9 11.7 1.0 N22 A:B121800 2.0 13.2 1.0 NE2 A:HIS610 2.3 11.3 1.0 O A:HOH2162 2.6 40.5 1.0 C9 A:B121800 2.8 14.6 1.0 C19 A:B121800 2.8 9.7 1.0 C16 A:B121800 2.9 6.2 1.0 C11 A:B121800 2.9 4.1 1.0 C1 A:B121800 2.9 10.7 1.0 C14 A:B121800 2.9 9.3 1.0 C4 A:B121800 2.9 12.1 1.0 C6 A:B121800 3.1 11.7 1.0 C10 A:B121800 3.2 7.1 1.0 CE1 A:HIS610 3.3 12.5 1.0 CD2 A:HIS610 3.3 12.4 1.0 C15 A:B121800 3.3 8.6 1.0 C5 A:B121800 3.4 8.3 1.0 C20 A:B121800 3.6 6.7 1.0 C18 A:B121800 4.1 10.9 1.0 C2 A:B121800 4.1 12.2 1.0 C17 A:B121800 4.2 12.0 1.0 C12 A:B121800 4.2 12.2 1.0 C13 A:B121800 4.2 10.1 1.0 C3 A:B121800 4.2 9.2 1.0 C8 A:B121800 4.2 12.6 1.0 C7 A:B121800 4.3 13.0 1.0 ND1 A:HIS610 4.4 13.8 1.0 CG A:HIS610 4.5 12.1 1.0 C26 A:B121800 4.5 7.5 1.0 O A:HOH2122 4.6 29.4 1.0 C42 A:B121800 4.6 15.7 1.0 C48 A:B121800 4.7 12.9 1.0 C54 A:B121800 4.7 9.6 1.0 C46 A:B121800 4.8 8.8 1.0 O A:HOH2138 4.8 33.8 1.0 C53 A:B121800 4.9 8.3 1.0 C35 A:B121800 4.9 10.8 1.0

Cobalt binding site 2 out of 2 in the Methylmalonyl-Coa Mutase, 2-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, 2-Carboxypropyl-Coa Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Co2800 b:10.0 occ:1.00 CO C:B122800 0.0 10.0 1.0 N23 C:B122800 1.8 10.7 1.0 N21 C:B122800 1.9 6.2 1.0 N24 C:B122800 1.9 12.4 1.0 N22 C:B122800 1.9 15.2 1.0 NE2 C:HIS610 2.5 14.3 1.0 O C:HOH3163 2.6 40.0 1.0 C11 C:B122800 2.8 8.1 1.0 C9 C:B122800 2.9 13.7 1.0 C1 C:B122800 2.9 10.2 1.0 C4 C:B122800 2.9 11.0 1.0 C16 C:B122800 2.9 7.0 1.0 C19 C:B122800 2.9 8.2 1.0 C14 C:B122800 2.9 10.4 1.0 C6 C:B122800 3.0 10.8 1.0 C10 C:B122800 3.2 12.8 1.0 C5 C:B122800 3.3 9.5 1.0 CD2 C:HIS610 3.4 13.8 1.0 C15 C:B122800 3.4 9.6 1.0 CE1 C:HIS610 3.5 14.3 1.0 C20 C:B122800 3.6 6.9 1.0 C18 C:B122800 4.1 10.1 1.0 C2 C:B122800 4.1 12.9 1.0 C12 C:B122800 4.2 11.2 1.0 C13 C:B122800 4.2 9.3 1.0 C3 C:B122800 4.2 9.7 1.0 C17 C:B122800 4.2 12.9 1.0 C8 C:B122800 4.2 12.7 1.0 C7 C:B122800 4.3 16.4 1.0 O C:HOH3121 4.4 25.1 1.0 C26 C:B122800 4.5 8.2 1.0 CG C:HIS610 4.6 15.4 1.0 ND1 C:HIS610 4.6 15.9 1.0 C42 C:B122800 4.6 19.1 1.0 C54 C:B122800 4.7 7.5 1.0 C46 C:B122800 4.7 4.1 1.0 C48 C:B122800 4.7 7.8 1.0 C35 C:B122800 4.9 8.2 1.0 C53 C:B122800 4.9 7.7 1.0 O C:HOH3138 4.9 38.4 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