Cobalt in PDB 9ccb: X-Ray Crystal Structure of Methyl-Coenzyme M Reductase Glutamine Methylase (Mgma) From Methanothermobacter Marburgensis with Hydroxycobalamin

The structure of X-Ray Crystal Structure of Methyl-Coenzyme M Reductase Glutamine Methylase (Mgma) From Methanothermobacter Marburgensis with Hydroxycobalamin, PDB code: 9ccb was solved by C.T.Lloyd, S.J.Booker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.93 / 2.08
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.7, 72.143, 114.868, 90, 90, 90
R / Rfree (%)	19.8 / 25

The structure of X-Ray Crystal Structure of Methyl-Coenzyme M Reductase Glutamine Methylase (Mgma) From Methanothermobacter Marburgensis with Hydroxycobalamin also contains other interesting chemical elements:

Calcium	(Ca)	2 atoms
Iron	(Fe)	4 atoms

The binding sites of Cobalt atom in the X-Ray Crystal Structure of Methyl-Coenzyme M Reductase Glutamine Methylase (Mgma) From Methanothermobacter Marburgensis with Hydroxycobalamin (pdb code 9ccb). 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 X-Ray Crystal Structure of Methyl-Coenzyme M Reductase Glutamine Methylase (Mgma) From Methanothermobacter Marburgensis with Hydroxycobalamin, PDB code: 9ccb:

Cobalt binding site 1 out of 1 in the X-Ray Crystal Structure of Methyl-Coenzyme M Reductase Glutamine Methylase (Mgma) From Methanothermobacter Marburgensis with Hydroxycobalamin


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of X-Ray Crystal Structure of Methyl-Coenzyme M Reductase Glutamine Methylase (Mgma) From Methanothermobacter Marburgensis with Hydroxycobalamin within 5.0Å range: probe atom residue distance (Å) B Occ A:Co502 b:20.9 occ:1.00 CO A:B12502 0.0 20.9 1.0 N24 A:B12502 1.9 22.9 1.0 N21 A:B12502 1.9 20.2 1.0 N23 A:B12502 1.9 23.3 1.0 N22 A:B12502 1.9 24.0 1.0 C9 A:B12502 2.9 27.3 1.0 C19 A:B12502 2.9 21.0 1.0 C1 A:B12502 2.9 21.5 1.0 C11 A:B12502 2.9 25.1 1.0 C14 A:B12502 3.0 23.7 1.0 C4 A:B12502 3.0 20.1 1.0 C16 A:B12502 3.0 22.0 1.0 C6 A:B12502 3.0 25.2 1.0 C10 A:B12502 3.2 24.9 1.0 C5 A:B12502 3.3 23.8 1.0 C15 A:B12502 3.3 23.2 1.0 C20 A:B12502 3.4 18.2 1.0 C18 A:B12502 4.1 21.8 1.0 C13 A:B12502 4.2 25.0 1.0 C2 A:B12502 4.2 20.6 1.0 C8 A:B12502 4.2 27.6 1.0 C3 A:B12502 4.2 21.8 1.0 C17 A:B12502 4.2 23.0 1.0 C12 A:B12502 4.2 26.2 1.0 C7 A:B12502 4.3 27.1 1.0 N52 A:B12502 4.3 25.8 1.0 C42 A:B12502 4.5 32.8 1.0 C48 A:B12502 4.5 25.3 1.0 C26 A:B12502 4.7 18.9 1.0 C35 A:B12502 4.7 23.7 1.0 C53 A:B12502 4.8 23.9 1.0 C46 A:B12502 4.8 25.7 1.0 O A:HOH695 4.9 24.5 1.0 C54 A:B12502 4.9 21.6 1.0 C41 A:B12502 5.0 30.6 1.0

C.T.Lloyd, S.J.Booker. Genetic and Biochemical Characterization of A Radical Sam Enzyme Required For Post-Translational Glutamine Methylation of Methyl-Coenzyme M Reductase To Be Published.