Cobalt in PDB 2xij: Crystal Structure of Human Methylmalonyl-Coa Mutase in Complex with Adenosylcobalamin

All present enzymatic activity of Crystal Structure of Human Methylmalonyl-Coa Mutase in Complex with Adenosylcobalamin:
5.4.99.2;

The structure of Crystal Structure of Human Methylmalonyl-Coa Mutase in Complex with Adenosylcobalamin, PDB code: 2xij was solved by W.W.Yue, D.S.Froese, G.Kochan, A.Chaikuad, T.Krojer, J.Muniz, M.Vollmar, C.Arrowsmith, J.Weigelt, A.Edwards, C.Bountra, U.Oppermann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	99.20 / 1.95
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	59.360, 137.720, 198.400, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 19.902

The binding sites of Cobalt atom in the Crystal Structure of Human Methylmalonyl-Coa Mutase in Complex with Adenosylcobalamin (pdb code 2xij). 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 Human Methylmalonyl-Coa Mutase in Complex with Adenosylcobalamin, PDB code: 2xij:

Cobalt binding site 1 out of 1 in the Crystal Structure of Human Methylmalonyl-Coa Mutase in Complex with Adenosylcobalamin


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 Human Methylmalonyl-Coa Mutase in Complex with Adenosylcobalamin within 5.0Å range: probe atom residue distance (Å) B Occ A:Co800 b:19.5 occ:1.00 CO A:B12800 0.0 19.5 1.0 N24 A:B12800 1.9 20.1 1.0 N21 A:B12800 1.9 18.4 1.0 N23 A:B12800 1.9 19.8 1.0 N22 A:B12800 2.0 24.3 1.0 NE2 A:HIS627 2.1 15.5 1.0 C5' A:5AD1746 2.2 16.6 1.0 C19 A:B12800 2.8 19.1 1.0 C1 A:B12800 2.8 20.0 1.0 C14 A:B12800 2.9 18.6 1.0 C4 A:B12800 2.9 21.0 1.0 C9 A:B12800 3.0 18.0 1.0 C11 A:B12800 3.0 19.9 1.0 C16 A:B12800 3.0 16.4 1.0 C6 A:B12800 3.0 22.5 1.0 CE1 A:HIS627 3.1 16.3 1.0 CD2 A:HIS627 3.1 16.9 1.0 C4' A:5AD1746 3.2 27.7 1.0 C5 A:B12800 3.4 20.6 1.0 C15 A:B12800 3.4 16.0 1.0 C10 A:B12800 3.4 20.0 1.0 C20 A:B12800 3.6 13.7 1.0 O4' A:5AD1746 3.8 41.5 1.0 C2 A:B12800 4.1 18.4 1.0 C18 A:B12800 4.1 19.2 1.0 C3 A:B12800 4.1 17.6 1.0 C13 A:B12800 4.1 16.2 1.0 ND1 A:HIS627 4.2 17.0 1.0 C8 A:B12800 4.2 21.2 1.0 C17 A:B12800 4.2 16.7 1.0 CG A:HIS627 4.3 17.8 1.0 C7 A:B12800 4.3 25.2 1.0 C12 A:B12800 4.4 23.3 1.0 C3' A:5AD1746 4.5 23.2 1.0 C26 A:B12800 4.6 17.5 1.0 C48 A:B12800 4.8 14.2 1.0 C41 A:B12800 4.9 27.6 1.0 C35 A:B12800 4.9 17.9 1.0 C46 A:B12800 4.9 20.6 1.0 C53 A:B12800 4.9 13.9 1.0 C54 A:B12800 5.0 17.9 1.0

D.S.Froese, G.Kochan, J.Muniz, X.Wu, C.Gileadi, E.Ugochukwu, E.Krysztofinska, R.A.Gravel, U.Oppermann, W.W.Yue. Structures of the Human Gtpase Mmaa and Vitamin B12-Dependent Methylmalonyl-Coa Mutase and Insight Into Their Complex Formation. J.Biol.Chem. V. 285 38204 2010.
ISSN: ISSN 0021-9258
PubMed: 20876572
DOI: 10.1074/JBC.M110.177717