Cobalt in PDB 6bnz: Crystal Structure of E144Q-Glyoxalase I Mutant From Zea Mays in Space Group P4(1)2(1)2

All present enzymatic activity of Crystal Structure of E144Q-Glyoxalase I Mutant From Zea Mays in Space Group P4(1)2(1)2:
4.4.1.5;

The structure of Crystal Structure of E144Q-Glyoxalase I Mutant From Zea Mays in Space Group P4(1)2(1)2, PDB code: 6bnz was solved by C.E.Alvarez, R.B.Agostini, J.M.Gonzalez, M.F.Drincovich, V.A.Camposbermudez, S.Klinke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.68 / 1.45
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	69.890, 69.890, 119.690, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 23.1

The binding sites of Cobalt atom in the Crystal Structure of E144Q-Glyoxalase I Mutant From Zea Mays in Space Group P4(1)2(1)2 (pdb code 6bnz). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of E144Q-Glyoxalase I Mutant From Zea Mays in Space Group P4(1)2(1)2, PDB code: 6bnz:

Cobalt binding site 1 out of 1 in the Crystal Structure of E144Q-Glyoxalase I Mutant From Zea Mays in Space Group P4(1)2(1)2


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of E144Q-Glyoxalase I Mutant From Zea Mays in Space Group P4(1)2(1)2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co301 b:21.6 occ:0.50 O A:HOH464 1.9 22.1 0.5 OE1 A:GLN157 2.1 19.8 1.0 O A:HOH477 2.1 23.8 0.5 OE1 A:GLN144 2.1 25.9 1.0 OE1 A:GLU208 2.1 24.8 1.0 NE2 A:HIS96 2.2 21.1 1.0 CE1 A:HIS96 2.8 18.6 1.0 CD A:GLN157 3.0 19.5 1.0 CD A:GLU208 3.2 23.9 1.0 CD A:GLN144 3.2 28.5 1.0 NE2 A:GLN157 3.3 20.8 1.0 CD2 A:HIS96 3.4 19.8 1.0 OE2 A:GLU208 3.5 29.0 1.0 NE2 A:GLN144 3.8 32.2 1.0 ND1 A:HIS96 4.0 19.4 1.0 CG A:HIS96 4.3 18.3 1.0 CG A:GLN157 4.4 19.4 1.0 CG A:GLN144 4.4 22.7 1.0 CG A:GLU208 4.5 20.1 1.0 CB A:GLN144 4.5 21.4 1.0 CD1 A:ILE146 4.6 21.6 1.0 CB A:MET159 4.6 15.5 1.0 CB A:GLN157 4.7 18.5 1.0 CG A:MET159 4.8 17.8 1.0 CB A:GLU208 4.8 19.2 1.0 CB A:ALA98 4.8 19.1 1.0 CE A:MET195 4.9 23.0 0.5 O A:HOH526 4.9 28.7 1.0

J.M.Gonzalez, R.B.Agostini, C.E.Alvarez, S.Klinke, C.S.Andreo, V.A.Campos-Bermudez. Deciphering the Number and Location of Active Sites in the Monomeric Glyoxalase I of Zea Mays. Febs J. V. 286 3255 2019.
ISSN: ISSN 1742-464X
PubMed: 30993890
DOI: 10.1111/FEBS.14855