Cobalt in PDB 1cb7: Glutamate Mutase From Clostridium Cochlearium Reconstituted with Methyl-Cobalamin

All present enzymatic activity of Glutamate Mutase From Clostridium Cochlearium Reconstituted with Methyl-Cobalamin:
5.4.99.1;

The structure of Glutamate Mutase From Clostridium Cochlearium Reconstituted with Methyl-Cobalamin, PDB code: 1cb7 was solved by K.Gruber, R.Reitzer, C.Kratky, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	64.330, 113.140, 108.610, 90.00, 95.62, 90.00
R / Rfree (%)	16 / 21.9

The binding sites of Cobalt atom in the Glutamate Mutase From Clostridium Cochlearium Reconstituted with Methyl-Cobalamin (pdb code 1cb7). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Glutamate Mutase From Clostridium Cochlearium Reconstituted with Methyl-Cobalamin, PDB code: 1cb7:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Glutamate Mutase From Clostridium Cochlearium Reconstituted with Methyl-Cobalamin


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Glutamate Mutase From Clostridium Cochlearium Reconstituted with Methyl-Cobalamin within 5.0Å range: probe atom residue distance (Å) B Occ A:Co800 b:11.6 occ:1.00 CO A:COB800 0.0 11.6 1.0 N21 A:COB800 1.9 9.5 1.0 N24 A:COB800 1.9 8.7 1.0 N23 A:COB800 1.9 10.7 1.0 N22 A:COB800 1.9 9.9 1.0 C1A A:COB800 2.0 11.1 0.7 NE2 A:HIS16 2.3 16.1 1.0 C19 A:COB800 2.8 9.3 1.0 C9 A:COB800 2.8 9.6 1.0 C1 A:COB800 2.9 12.2 1.0 C11 A:COB800 2.9 11.8 1.0 C4 A:COB800 2.9 10.8 1.0 C14 A:COB800 2.9 11.2 1.0 C16 A:COB800 2.9 10.9 1.0 C6 A:COB800 3.0 10.3 1.0 CE1 A:HIS16 3.2 13.9 1.0 C10 A:COB800 3.2 14.3 1.0 C5 A:COB800 3.3 9.4 1.0 C15 A:COB800 3.4 8.4 1.0 C1A A:COB800 3.4 11.1 0.4 CD2 A:HIS16 3.4 14.4 1.0 C20 A:COB800 3.6 10.9 1.0 C18 A:COB800 4.1 9.0 1.0 C2 A:COB800 4.1 13.2 1.0 C3 A:COB800 4.1 11.7 1.0 C8 A:COB800 4.2 8.7 1.0 C13 A:COB800 4.2 11.4 1.0 C17 A:COB800 4.2 9.2 1.0 C12 A:COB800 4.2 12.4 1.0 C7 A:COB800 4.2 12.8 1.0 ND1 A:HIS16 4.4 14.5 1.0 O A:HOH863 4.4 39.2 1.0 C26 A:COB800 4.5 15.4 1.0 CG A:HIS16 4.5 13.7 1.0 C37 A:COB800 4.6 16.6 1.0 O39 A:COB800 4.7 18.3 1.0 C48 A:COB800 4.8 13.5 1.0 C53 A:COB800 4.9 9.2 1.0 C46 A:COB800 4.9 7.5 1.0 C35 A:COB800 4.9 15.3 1.0 O B:HOH942 4.9 11.6 1.0 C54 A:COB800 4.9 12.1 1.0 C41 A:COB800 4.9 12.4 1.0

Cobalt binding site 2 out of 2 in the Glutamate Mutase From Clostridium Cochlearium Reconstituted with Methyl-Cobalamin


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Glutamate Mutase From Clostridium Cochlearium Reconstituted with Methyl-Cobalamin within 5.0Å range: probe atom residue distance (Å) B Occ C:Co800 b:12.4 occ:1.00 CO C:COB800 0.0 12.4 1.0 N21 C:COB800 1.9 8.7 1.0 N24 C:COB800 1.9 9.3 1.0 N23 C:COB800 1.9 9.3 1.0 N22 C:COB800 1.9 10.3 1.0 C1A C:COB800 2.0 11.1 0.7 NE2 C:HIS16 2.3 15.9 1.0 C19 C:COB800 2.8 8.5 1.0 C9 C:COB800 2.8 9.7 1.0 C11 C:COB800 2.9 12.0 1.0 C1 C:COB800 2.9 11.2 1.0 C4 C:COB800 2.9 10.6 1.0 C14 C:COB800 2.9 9.6 1.0 C16 C:COB800 2.9 9.9 1.0 C6 C:COB800 3.0 10.9 1.0 C10 C:COB800 3.2 12.3 1.0 CE1 C:HIS16 3.2 20.2 1.0 C5 C:COB800 3.3 9.6 1.0 C15 C:COB800 3.3 8.1 1.0 C1A C:COB800 3.4 11.1 0.4 CD2 C:HIS16 3.4 13.6 1.0 C20 C:COB800 3.6 10.3 1.0 C2 C:COB800 4.1 12.8 1.0 C18 C:COB800 4.1 10.0 1.0 C8 C:COB800 4.1 10.3 1.0 C3 C:COB800 4.2 11.4 1.0 C13 C:COB800 4.2 10.9 1.0 C12 C:COB800 4.2 10.4 1.0 C7 C:COB800 4.2 13.9 1.0 C17 C:COB800 4.2 10.3 1.0 ND1 C:HIS16 4.4 16.9 1.0 C26 C:COB800 4.5 14.5 1.0 CG C:HIS16 4.5 14.1 1.0 C37 C:COB800 4.6 15.9 1.0 O39 C:COB800 4.6 18.8 1.0 O C:HOH826 4.7 25.7 1.0 C48 C:COB800 4.8 14.1 1.0 C46 C:COB800 4.8 7.2 1.0 C53 C:COB800 4.8 8.3 1.0 C35 C:COB800 4.9 15.3 1.0 C54 C:COB800 4.9 13.1 1.0 C38 C:COB800 4.9 20.4 1.0 C41 C:COB800 4.9 12.8 1.0 O D:HOH927 4.9 12.2 1.0

R.Reitzer, K.Gruber, G.Jogl, U.G.Wagner, H.Bothe, W.Buckel, C.Kratky. Glutamate Mutase From Clostridium Cochlearium: the Structure of A Coenzyme B12-Dependent Enzyme Provides New Mechanistic Insights. Structure Fold.Des. V. 7 891 1999.
ISSN: ISSN 0969-2126
PubMed: 10467146
DOI: 10.1016/S0969-2126(99)80116-6