Cobalt in PDB 5ujc: Crystal Structure of A C.Elegans B12-Trafficking Protein Cblc, A Human Mmachc Homologue

The structure of Crystal Structure of A C.Elegans B12-Trafficking Protein Cblc, A Human Mmachc Homologue, PDB code: 5ujc was solved by Z.Li, A.Shanmuganathan, M.Ruetz, K.Yamada, N.A.Lesniak, B.Krautler, T.C.Brunold, R.Banerjee, M.Koutmos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	53.84 / 1.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.008, 66.089, 92.826, 90.00, 90.00, 90.00
R / Rfree (%)	13.2 / 16.3

The binding sites of Cobalt atom in the Crystal Structure of A C.Elegans B12-Trafficking Protein Cblc, A Human Mmachc Homologue (pdb code 5ujc). 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 A C.Elegans B12-Trafficking Protein Cblc, A Human Mmachc Homologue, PDB code: 5ujc:

Cobalt binding site 1 out of 1 in the Crystal Structure of A C.Elegans B12-Trafficking Protein Cblc, A Human Mmachc Homologue


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 A C.Elegans B12-Trafficking Protein Cblc, A Human Mmachc Homologue within 5.0Å range: probe atom residue distance (Å) B Occ A:Co300 b:8.9 occ:1.00 CO A:COB300 0.0 8.9 1.0 N21 A:COB300 1.9 7.7 1.0 N24 A:COB300 1.9 8.7 1.0 N22 A:COB300 1.9 8.7 1.0 N23 A:COB300 1.9 9.4 1.0 C1A A:COB300 2.0 11.7 1.0 C19 A:COB300 2.7 8.6 1.0 C1 A:COB300 2.8 7.2 1.0 C9 A:COB300 2.8 9.4 1.0 C11 A:COB300 2.9 10.2 1.0 C4 A:COB300 2.9 7.6 1.0 C6 A:COB300 2.9 8.8 1.0 C14 A:COB300 2.9 9.4 1.0 C16 A:COB300 3.0 9.3 1.0 H202 A:COB300 3.1 8.0 1.0 C10 A:COB300 3.2 10.0 1.0 C5 A:COB300 3.3 7.3 1.0 C15 A:COB300 3.4 9.4 1.0 C20 A:COB300 3.5 8.0 1.0 H422 A:COB300 3.6 11.4 1.0 H203 A:COB300 3.9 8.0 1.0 H261 A:COB300 3.9 7.5 1.0 H492 A:COB300 3.9 12.0 1.0 C2 A:COB300 4.1 7.3 1.0 C18 A:COB300 4.1 7.7 1.0 C8 A:COB300 4.2 9.2 1.0 C12 A:COB300 4.2 10.4 1.0 C3 A:COB300 4.2 7.8 1.0 H10 A:COB300 4.2 10.0 1.0 C13 A:COB300 4.2 10.4 1.0 C7 A:COB300 4.2 8.6 1.0 C17 A:COB300 4.2 8.6 1.0 HD11 A:ILE172 4.2 13.0 1.0 H462 A:COB300 4.3 11.6 1.0 H371 A:COB300 4.3 8.3 1.0 H201 A:COB300 4.3 8.0 1.0 HD13 A:ILE172 4.4 13.0 1.0 H491 A:COB300 4.4 12.0 1.0 C26 A:COB300 4.4 7.5 1.0 C42 A:COB300 4.5 11.4 1.0 C49 A:COB300 4.6 12.0 1.0 H18 A:COB300 4.6 7.7 1.0 H561 A:COB300 4.6 11.4 1.0 C46 A:COB300 4.7 11.6 1.0 H542 A:COB300 4.7 10.4 1.0 H262 A:COB300 4.7 7.5 1.0 CD1 A:ILE172 4.7 13.0 1.0 HD12 A:ILE172 4.8 13.0 1.0 C37 A:COB300 4.8 8.3 1.0 H463 A:COB300 4.8 11.6 1.0 H3 A:COB300 4.8 7.8 1.0 C35 A:COB300 4.9 8.5 1.0 C53 A:COB300 4.9 10.4 1.0 C41 A:COB300 4.9 9.5 1.0 H11 A:GOL304 4.9 37.7 1.0 H8 A:COB300 4.9 9.2 1.0 H421 A:COB300 4.9 11.4 1.0 H13 A:COB300 5.0 10.4 1.0 HZ A:PHE222 5.0 11.4 1.0

Z.Li, A.Shanmuganathan, M.Ruetz, K.Yamada, N.A.Lesniak, B.Krautler, T.C.Brunold, M.Koutmos, R.Banerjee. Coordination Chemistry Controls the Thiol Oxidase Activity of the B12-Trafficking Protein Cblc. J. Biol. Chem. V. 292 9733 2017.
ISSN: ESSN 1083-351X
PubMed: 28442570
DOI: 10.1074/JBC.M117.788554