Cobalt in PDB 5iav: Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding By An Unusual Bacterial Prolyl Hydroxylase - Co- BAP4H-Mli

The structure of Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding By An Unusual Bacterial Prolyl Hydroxylase - Co- BAP4H-Mli, PDB code: 5iav was solved by N.J.Schnicker, M.Dey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.68 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.769, 41.495, 111.043, 90.00, 96.67, 90.00
R / Rfree (%)	21.2 / 22.9

The binding sites of Cobalt atom in the Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding By An Unusual Bacterial Prolyl Hydroxylase - Co- BAP4H-Mli (pdb code 5iav). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding By An Unusual Bacterial Prolyl Hydroxylase - Co- BAP4H-Mli, PDB code: 5iav:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding By An Unusual Bacterial Prolyl Hydroxylase - Co- BAP4H-Mli


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding By An Unusual Bacterial Prolyl Hydroxylase - Co- BAP4H-Mli within 5.0Å range: probe atom residue distance (Å) B Occ A:Co301 b:17.9 occ:1.00 OD1 A:ASP129 2.1 17.8 1.0 NE2 A:HIS127 2.1 14.8 1.0 NE2 A:HIS193 2.1 15.8 1.0 O A:HOH495 2.1 21.0 1.0 O A:HOH506 2.4 27.5 1.0 O6 A:MLI302 2.6 26.3 1.0 CG A:ASP129 3.0 13.9 1.0 CE1 A:HIS193 3.0 15.1 1.0 CE1 A:HIS127 3.0 17.7 1.0 CD2 A:HIS127 3.1 16.7 1.0 CD2 A:HIS193 3.1 13.8 1.0 OD2 A:ASP129 3.2 14.6 1.0 O A:HOH494 3.9 21.1 1.0 C2 A:MLI302 3.9 22.4 1.0 ND1 A:HIS127 4.1 20.2 1.0 ND1 A:HIS193 4.1 15.8 1.0 CG A:HIS127 4.2 17.0 1.0 CG A:HIS193 4.2 14.8 1.0 CB A:ASP129 4.4 13.4 1.0 O7 A:MLI302 4.7 30.0 1.0 NE1 A:TRP209 4.7 18.1 1.0 CA A:ASP129 4.8 13.3 1.0 C1 A:MLI302 4.8 24.3 1.0 CZ A:PHE178 4.8 13.3 1.0 N A:ASP129 4.9 13.8 1.0

Cobalt binding site 2 out of 2 in the Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding By An Unusual Bacterial Prolyl Hydroxylase - Co- BAP4H-Mli


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding By An Unusual Bacterial Prolyl Hydroxylase - Co- BAP4H-Mli within 5.0Å range: probe atom residue distance (Å) B Occ B:Co301 b:32.9 occ:1.00 OD1 B:ASP129 2.1 30.8 1.0 NE2 B:HIS127 2.1 21.8 1.0 NE2 B:HIS193 2.2 19.9 1.0 O B:HOH476 2.3 27.3 1.0 O B:HOH487 2.7 28.7 1.0 O7 B:MLI302 2.7 32.2 1.0 CG B:ASP129 3.0 28.9 1.0 CE1 B:HIS127 3.0 26.7 1.0 OD2 B:ASP129 3.1 24.3 1.0 CE1 B:HIS193 3.2 20.1 1.0 CD2 B:HIS127 3.2 25.9 1.0 CD2 B:HIS193 3.2 23.4 1.0 O B:HOH449 3.8 28.5 1.0 C2 B:MLI302 3.9 30.5 1.0 ND1 B:HIS127 4.2 24.9 1.0 CG B:HIS127 4.3 28.1 1.0 ND1 B:HIS193 4.3 25.3 1.0 CG B:HIS193 4.3 20.5 1.0 CB B:ASP129 4.4 31.6 1.0 NE1 B:TRP209 4.7 28.7 1.0 O6 B:MLI302 4.7 31.9 1.0 CA B:ASP129 4.8 29.1 1.0 C1 B:MLI302 4.9 29.7 1.0 CZ B:PHE178 4.9 18.8 1.0 CZ2 B:TRP209 5.0 27.7 1.0

N.J.Schnicker, M.Dey. Bacillus Anthracis Prolyl 4-Hydroxylase Modifies Collagen-Like Substrates in Asymmetric Patterns. J.Biol.Chem. V. 291 13360 2016.
ISSN: ESSN 1083-351X
PubMed: 27129244
DOI: 10.1074/JBC.M116.725432