Cobalt in PDB 2ycl: Complete Structure of the Corrinoid,Iron-Sulfur Protein Including the N-Terminal Domain with A 4FE-4S Cluster

The structure of Complete Structure of the Corrinoid,Iron-Sulfur Protein Including the N-Terminal Domain with A 4FE-4S Cluster, PDB code: 2ycl was solved by S.Goetzl, J.H.Jeoung, S.E.Hennig, H.Dobbek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.745 / 1.95
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	172.219, 43.476, 101.855, 90.00, 119.39, 90.00
R / Rfree (%)	19.15 / 25.14

The structure of Complete Structure of the Corrinoid,Iron-Sulfur Protein Including the N-Terminal Domain with A 4FE-4S Cluster also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Cobalt atom in the Complete Structure of the Corrinoid,Iron-Sulfur Protein Including the N-Terminal Domain with A 4FE-4S Cluster (pdb code 2ycl). 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 Complete Structure of the Corrinoid,Iron-Sulfur Protein Including the N-Terminal Domain with A 4FE-4S Cluster, PDB code: 2ycl:

Cobalt binding site 1 out of 1 in the Complete Structure of the Corrinoid,Iron-Sulfur Protein Including the N-Terminal Domain with A 4FE-4S Cluster


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Complete Structure of the Corrinoid,Iron-Sulfur Protein Including the N-Terminal Domain with A 4FE-4S Cluster within 5.0Å range: probe atom residue distance (Å) B Occ A:Co1442 b:19.1 occ:1.00 CO A:B121442 0.0 19.1 1.0 N24 A:B121442 1.9 14.9 1.0 N22 A:B121442 1.9 18.4 1.0 N21 A:B121442 1.9 19.4 1.0 N23 A:B121442 2.0 11.7 1.0 O A:HOH2506 2.6 15.4 1.0 C16 A:B121442 2.8 15.7 1.0 C19 A:B121442 2.9 18.9 1.0 C11 A:B121442 2.9 16.2 1.0 C1 A:B121442 2.9 20.0 1.0 C9 A:B121442 3.0 17.2 1.0 C6 A:B121442 3.0 18.5 1.0 C4 A:B121442 3.0 20.8 1.0 C14 A:B121442 3.0 19.5 1.0 OG1 A:THR374 3.2 19.9 1.0 C15 A:B121442 3.3 16.1 1.0 C10 A:B121442 3.3 18.2 1.0 C5 A:B121442 3.4 21.7 1.0 C20 A:B121442 3.5 18.5 1.0 C3 A:B121442 4.0 24.3 1.0 C8 A:B121442 4.1 19.4 1.0 C17 A:B121442 4.1 15.8 1.0 C2 A:B121442 4.1 22.1 1.0 C13 A:B121442 4.2 15.1 1.0 C12 A:B121442 4.2 15.6 1.0 C18 A:B121442 4.2 15.6 1.0 C7 A:B121442 4.2 20.6 1.0 CB A:THR374 4.2 22.9 1.0 CG2 A:THR374 4.3 18.9 1.0 O B:HOH2202 4.6 19.4 1.0 O B:HOH2176 4.6 21.5 1.0 C46 A:B121442 4.6 13.1 1.0 C26 A:B121442 4.7 23.0 1.0 CA A:THR374 4.7 17.1 1.0 C53 A:B121442 4.7 15.8 1.0 C48 A:B121442 4.9 21.0 1.0 C37 A:B121442 4.9 20.7 1.0 C54 A:B121442 4.9 18.2 1.0 C35 A:B121442 5.0 17.9 1.0

S.Goetzl, J.H.Jeoung, S.E.Hennig, H.Dobbek. Structural Basis For Electron and Methyl-Group Transfer in A Methyltransferase System Operating in the Reductive Acetyl-Coa Pathway J.Mol.Biol. V. 411 96 2011.
ISSN: ISSN 0022-2836
PubMed: 21640123
DOI: 10.1016/J.JMB.2011.05.025