Cobalt in PDB 5v8c: Lytr-CSP2A-Psr Enzyme From Actinomyces Oris

The structure of Lytr-CSP2A-Psr Enzyme From Actinomyces Oris, PDB code: 5v8c was solved by B.R.Amer, M.R.Sawaya, B.Liauw, J.Y.Fu, H.Ton-That, R.T.Clubb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.83 / 2.51
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.850, 69.070, 82.010, 90.00, 90.00, 90.00
R / Rfree (%)	22.1 / 27.2

The binding sites of Cobalt atom in the Lytr-CSP2A-Psr Enzyme From Actinomyces Oris (pdb code 5v8c). 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 Lytr-CSP2A-Psr Enzyme From Actinomyces Oris, PDB code: 5v8c:

Cobalt binding site 1 out of 1 in the Lytr-CSP2A-Psr Enzyme From Actinomyces Oris


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Lytr-CSP2A-Psr Enzyme From Actinomyces Oris within 5.0Å range: probe atom residue distance (Å) B Occ A:Co401 b:0.2 occ:1.00 N A:HIS79 2.1 0.3 1.0 N A:ALA78 2.2 0.5 1.0 NE2 A:HIS296 2.4 94.7 1.0 ND1 A:HIS79 2.7 0.1 1.0 CA A:ALA78 2.8 0.5 1.0 C A:ALA78 2.8 0.1 1.0 CG A:HIS79 3.1 0.1 1.0 CA A:HIS79 3.1 0.2 1.0 CE1 A:HIS296 3.2 94.5 1.0 CB A:HIS79 3.4 0.3 1.0 CB A:ALA78 3.4 0.1 1.0 CD2 A:HIS296 3.4 93.4 1.0 CE1 A:HIS79 3.5 0.7 1.0 O A:ALA78 4.0 1.0 1.0 CD2 A:HIS79 4.0 0.3 1.0 NE2 A:HIS79 4.2 0.2 1.0 ND1 A:HIS296 4.4 94.0 1.0 CG A:HIS296 4.5 91.6 1.0 C A:HIS79 4.5 0.6 1.0 O A:HIS79 5.0 98.1 1.0

S.D.Siegel, B.R.Amer, C.Wu, M.R.Sawaya, J.E.Gosschalk, R.T.Clubb, H.Ton-That. Structure and Mechanism of Lcpa, A Phosphotransferase That Mediates Glycosylation of A Gram-Positive Bacterial Cell Wall-Anchored Protein. Mbio V. 10 2019.
ISSN: ESSN 2150-7511
PubMed: 30782654
DOI: 10.1128/MBIO.01580-18