Cobalt in PDB 3sc0: Crystal Structure of Mmachc (1-238), A Human B12 Processing Enzyme, Complexed with Methylcobalamin

The structure of Crystal Structure of Mmachc (1-238), A Human B12 Processing Enzyme, Complexed with Methylcobalamin, PDB code: 3sc0 was solved by M.Koutmos, C.Gherasim, J.L.Smith, R.Banerjee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.29 / 1.95
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	105.955, 105.955, 84.253, 90.00, 90.00, 120.00
R / Rfree (%)	18.6 / 24.4

The binding sites of Cobalt atom in the Crystal Structure of Mmachc (1-238), A Human B12 Processing Enzyme, Complexed with Methylcobalamin (pdb code 3sc0). 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 Mmachc (1-238), A Human B12 Processing Enzyme, Complexed with Methylcobalamin, PDB code: 3sc0:

Cobalt binding site 1 out of 1 in the Crystal Structure of Mmachc (1-238), A Human B12 Processing Enzyme, Complexed with Methylcobalamin


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 Mmachc (1-238), A Human B12 Processing Enzyme, Complexed with Methylcobalamin within 5.0Å range: probe atom residue distance (Å) B Occ A:Co300 b:18.1 occ:1.00 CO A:COB300 0.0 18.1 1.0 N24 A:COB300 1.7 19.9 1.0 N23 A:COB300 1.7 24.1 1.0 N22 A:COB300 1.8 23.5 1.0 N21 A:COB300 1.8 16.8 1.0 C1A A:COB300 2.0 20.2 1.0 C19 A:COB300 2.5 16.8 1.0 C1 A:COB300 2.6 14.8 1.0 C14 A:COB300 2.6 23.9 1.0 C9 A:COB300 2.6 26.8 1.0 C6 A:COB300 2.7 24.3 1.0 C16 A:COB300 2.7 19.1 1.0 C11 A:COB300 2.7 23.9 1.0 C4 A:COB300 2.7 17.1 1.0 C15 A:COB300 3.0 23.9 1.0 H202 A:COB300 3.0 18.6 1.0 C10 A:COB300 3.1 23.7 1.0 C5 A:COB300 3.1 19.7 1.0 C20 A:COB300 3.3 15.5 1.0 H521 A:COB300 3.4 32.2 1.0 H451 A:COB300 3.7 22.3 1.0 H203 A:COB300 3.8 18.6 1.0 C18 A:COB300 4.0 22.7 1.0 N52 A:COB300 4.0 26.9 1.0 H10 A:COB300 4.0 28.4 1.0 C2 A:COB300 4.0 17.6 1.0 C7 A:COB300 4.0 30.7 1.0 C8 A:COB300 4.0 24.3 1.0 C3 A:COB300 4.0 20.8 1.0 C12 A:COB300 4.0 31.7 1.0 C17 A:COB300 4.0 21.5 1.0 C13 A:COB300 4.0 27.8 1.0 H261 A:COB300 4.1 20.1 1.0 H201 A:COB300 4.1 18.6 1.0 N45 A:COB300 4.1 18.6 1.0 H372 A:COB300 4.2 38.6 1.0 H522 A:COB300 4.2 32.2 1.0 H452 A:COB300 4.2 22.3 1.0 H412 A:COB300 4.4 29.2 1.0 H482 A:COB300 4.5 36.5 1.0 H462 A:COB300 4.5 35.7 1.0 H542 A:COB300 4.5 17.1 1.0 C26 A:COB300 4.5 16.8 1.0 C53 A:COB300 4.5 26.3 1.0 C35 A:COB300 4.6 22.6 1.0 C37 A:COB300 4.6 32.2 1.0 H8 A:COB300 4.6 29.1 1.0 HZ A:PHE196 4.6 27.6 1.0 H3 A:COB300 4.7 24.9 1.0 H561 A:COB300 4.7 26.7 1.0 H13 A:COB300 4.7 33.4 1.0 H262 A:COB300 4.7 20.1 1.0 C46 A:COB300 4.8 29.8 1.0 C41 A:COB300 4.8 24.4 1.0 C48 A:COB300 4.8 30.4 1.0 C54 A:COB300 4.9 14.2 1.0 H533 A:COB300 4.9 31.6 1.0 O39 A:COB300 4.9 33.2 1.0 H463 A:COB300 4.9 35.7 1.0 H532 A:COB300 4.9 31.6 1.0 C50 A:COB300 4.9 30.9 1.0 H302 A:COB300 5.0 20.5 1.0 H353 A:COB300 5.0 27.1 1.0 H473 A:COB300 5.0 35.8 1.0 H491 A:COB300 5.0 54.0 1.0 H352 A:COB300 5.0 27.1 1.0

M.Koutmos, C.Gherasim, J.L.Smith, R.Banerjee. Structural Basis of Multifunctionality in A Vitamin B12-Processing Enzyme. J.Biol.Chem. V. 286 29780 2011.
ISSN: ISSN 0021-9258
PubMed: 21697092
DOI: 10.1074/JBC.M111.261370