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

The structure of Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding By An Unusual Bacterial Prolyl Hydroxylase - Co- BAP4H-Ppg, PDB code: 5iax 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)	61.48 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.791, 75.553, 105.768, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 23.4

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-Ppg (pdb code 5iax). 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-Ppg, PDB code: 5iax:
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-Ppg


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-Ppg within 5.0Å range: probe atom residue distance (Å) B Occ A:Co301 b:18.9 occ:1.00 O1 A:AKG302 2.0 27.9 1.0 NE2 A:HIS193 2.0 21.2 1.0 OD1 A:ASP129 2.1 20.8 1.0 O5 A:AKG302 2.1 24.5 1.0 NE2 A:HIS127 2.1 23.5 1.0 C1 A:AKG302 2.7 24.0 1.0 C2 A:AKG302 2.7 23.6 1.0 CG A:ASP129 2.9 22.5 1.0 OD2 A:ASP129 3.0 23.5 1.0 CD2 A:HIS193 3.0 22.8 1.0 CE1 A:HIS193 3.0 22.6 1.0 CE1 A:HIS127 3.1 25.2 1.0 CD2 A:HIS127 3.1 21.7 1.0 O A:HOH440 3.8 31.8 1.0 O2 A:AKG302 3.9 26.7 1.0 ND1 A:HIS193 4.1 20.8 1.0 CG A:HIS193 4.1 20.6 1.0 ND1 A:HIS127 4.2 26.6 1.0 CG A:HIS127 4.2 26.0 1.0 C3 A:AKG302 4.3 23.5 1.0 CB A:ASP129 4.3 21.1 1.0 CE2 A:TYR124 4.4 30.5 1.0 NE1 A:TRP209 4.5 25.3 1.0 CZ A:TYR124 4.6 33.6 1.0 OH A:TYR124 4.7 40.2 1.0 CZ A:PHE178 4.7 19.6 1.0 CA A:ASP129 4.7 23.8 1.0 C4 A:AKG302 4.9 21.4 1.0 N A:ASP129 4.9 22.2 1.0 CD2 A:TYR124 5.0 27.9 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-Ppg


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-Ppg within 5.0Å range: probe atom residue distance (Å) B Occ B:Co301 b:19.9 occ:1.00 O2 B:AKG302 1.9 27.3 1.0 NE2 B:HIS193 2.1 25.1 1.0 OD1 B:ASP129 2.1 22.3 1.0 NE2 B:HIS127 2.1 21.3 1.0 O5 B:AKG302 2.2 25.9 1.0 C1 B:AKG302 2.6 27.0 1.0 C2 B:AKG302 2.7 23.3 1.0 CG B:ASP129 3.0 26.6 1.0 CE1 B:HIS193 3.0 24.8 1.0 CD2 B:HIS193 3.0 24.1 1.0 CD2 B:HIS127 3.1 24.6 1.0 CE1 B:HIS127 3.1 24.8 1.0 OD2 B:ASP129 3.2 27.6 1.0 O1 B:AKG302 3.8 28.6 1.0 ND1 B:HIS193 4.1 23.1 1.0 CG B:HIS193 4.1 25.6 1.0 CG B:HIS127 4.2 26.8 1.0 ND1 B:HIS127 4.2 26.8 1.0 C3 B:AKG302 4.3 21.5 1.0 CB B:ASP129 4.3 26.1 1.0 CE2 B:TYR124 4.4 31.7 1.0 NE1 B:TRP209 4.5 29.4 1.0 OH B:TYR124 4.7 39.1 1.0 CZ B:TYR124 4.7 35.1 1.0 CA B:ASP129 4.7 24.6 1.0 CZ B:PHE178 4.7 23.6 1.0 N B:ASP129 4.8 26.3 1.0 C4 B:AKG302 5.0 23.7 1.0 CD2 B:TYR124 5.0 29.0 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