Cobalt in PDB 1i9c: Glutamate Mutase From Clostridium Cochlearium: Complex with Adenosylcobalamin and Substrate

All present enzymatic activity of Glutamate Mutase From Clostridium Cochlearium: Complex with Adenosylcobalamin and Substrate:
5.4.99.1;

The structure of Glutamate Mutase From Clostridium Cochlearium: Complex with Adenosylcobalamin and Substrate, PDB code: 1i9c was solved by K.Gruber, C.Kratky, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	64.348, 113.139, 108.439, 90.00, 96.00, 90.00
R / Rfree (%)	16.8 / 22.1

The binding sites of Cobalt atom in the Glutamate Mutase From Clostridium Cochlearium: Complex with Adenosylcobalamin and Substrate (pdb code 1i9c). 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: Complex with Adenosylcobalamin and Substrate, PDB code: 1i9c:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Glutamate Mutase From Clostridium Cochlearium: Complex with Adenosylcobalamin and Substrate


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: Complex with Adenosylcobalamin and Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Co800 b:7.6 occ:1.00 CO A:B12800 0.0 7.6 1.0 N21 A:B12800 1.9 6.9 1.0 N24 A:B12800 1.9 5.6 1.0 N23 A:B12800 1.9 5.9 1.0 N22 A:B12800 2.0 5.0 1.0 NE2 A:HIS16 2.2 12.2 1.0 C19 A:B12800 2.8 3.5 1.0 C1 A:B12800 2.9 4.7 1.0 C4 A:B12800 2.9 7.9 1.0 C11 A:B12800 2.9 6.1 1.0 C14 A:B12800 2.9 0.9 1.0 C16 A:B12800 2.9 4.6 1.0 C6 A:B12800 3.0 7.0 1.0 C9 A:B12800 3.0 8.5 1.0 CE1 A:HIS16 3.1 7.3 1.0 C5' B:5AD1303 3.2 12.1 0.4 C10 A:B12800 3.2 7.5 1.0 CD2 A:HIS16 3.3 1.8 1.0 C15 A:B12800 3.3 6.6 1.0 C5 A:B12800 3.4 9.4 1.0 C20 A:B12800 3.5 7.2 1.0 O3' B:5AD1303 3.7 12.1 0.6 C3' B:5AD1303 4.1 12.1 0.6 C18 A:B12800 4.1 1.0 1.0 C2 A:B12800 4.1 1.8 1.0 C3 A:B12800 4.2 3.8 1.0 C13 A:B12800 4.2 7.7 1.0 C5' B:5AD1303 4.2 12.1 0.6 C17 A:B12800 4.2 6.6 1.0 C12 A:B12800 4.2 7.8 1.0 C7 A:B12800 4.2 8.5 1.0 ND1 A:HIS16 4.3 5.1 1.0 C8 A:B12800 4.3 7.2 1.0 CG A:HIS16 4.4 5.1 1.0 C26 A:B12800 4.6 5.4 1.0 C4' B:5AD1303 4.6 12.1 0.4 C48 A:B12800 4.7 10.7 1.0 C4' B:5AD1303 4.8 12.1 0.6 O B:HOH1330 4.8 7.1 1.0 C35 A:B12800 4.8 17.1 1.0 C53 A:B12800 4.8 7.5 1.0 C46 A:B12800 4.8 5.4 1.0 C54 A:B12800 4.8 7.8 1.0 C41 A:B12800 5.0 9.5 1.0

Cobalt binding site 2 out of 2 in the Glutamate Mutase From Clostridium Cochlearium: Complex with Adenosylcobalamin and Substrate


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: Complex with Adenosylcobalamin and Substrate within 5.0Å range: probe atom residue distance (Å) B Occ C:Co800 b:7.2 occ:1.00 CO C:B12800 0.0 7.2 1.0 N21 C:B12800 1.9 3.0 1.0 N24 C:B12800 1.9 3.7 1.0 N23 C:B12800 1.9 7.2 1.0 N22 C:B12800 2.0 6.6 1.0 NE2 C:HIS16 2.2 5.5 1.0 C19 C:B12800 2.8 4.7 1.0 C1 C:B12800 2.9 5.5 1.0 C11 C:B12800 2.9 6.7 1.0 C4 C:B12800 2.9 7.4 1.0 C14 C:B12800 2.9 9.6 1.0 C16 C:B12800 2.9 5.1 1.0 C6 C:B12800 3.0 6.7 1.0 C9 C:B12800 3.0 3.9 1.0 CE1 C:HIS16 3.1 2.6 1.0 C5' D:5AD1304 3.2 12.1 0.4 C10 C:B12800 3.3 4.9 1.0 CD2 C:HIS16 3.3 4.3 1.0 C15 C:B12800 3.3 3.7 1.0 C5 C:B12800 3.4 10.1 1.0 C20 C:B12800 3.6 10.3 1.0 O3' D:5AD1304 3.8 12.1 0.6 C18 C:B12800 4.1 4.0 1.0 C3' D:5AD1304 4.1 12.1 0.6 C2 C:B12800 4.1 3.2 1.0 C3 C:B12800 4.2 4.6 1.0 C13 C:B12800 4.2 12.3 1.0 C5' D:5AD1304 4.2 12.1 0.6 C17 C:B12800 4.2 4.5 1.0 C12 C:B12800 4.2 7.5 1.0 ND1 C:HIS16 4.2 2.6 1.0 C7 C:B12800 4.3 11.0 1.0 C8 C:B12800 4.3 5.5 1.0 CG C:HIS16 4.4 6.3 1.0 C26 C:B12800 4.5 6.2 1.0 C4' D:5AD1304 4.6 12.1 0.4 C48 C:B12800 4.7 10.2 1.0 O D:HOH1314 4.8 4.8 1.0 C4' D:5AD1304 4.8 12.1 0.6 C53 C:B12800 4.8 7.7 1.0 C35 C:B12800 4.8 13.3 1.0 C46 C:B12800 4.8 9.9 1.0 C54 C:B12800 4.9 5.7 1.0 C41 C:B12800 5.0 10.5 1.0

K.Gruber, R.Reitzer, C.Kratky. Radical Shuttling in A Protein: Ribose Pseudorotation Controls Alkyl-Radical Transfer in the Coenzyme B(12) Dependent Enzyme Glutamate Mutase Angew.Chem.Int.Ed.Engl. V. 40 3377 2001.
ISSN: ISSN 1433-7851
PubMed: 11592143
DOI: 10.1002/1521-3773(20010917)40:18<3377::AID-ANIE3377>3.0.CO;2-8