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Cobalt in PDB 3iv9: Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half in A "His-on" Conformation

Enzymatic activity of Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half in A "His-on" Conformation

All present enzymatic activity of Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half in A "His-on" Conformation:
2.1.1.13;

Protein crystallography data

The structure of Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half in A "His-on" Conformation, PDB code: 3iv9 was solved by K.A.Pattridge, M.Koutmos, J.L.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.10 / 3.25
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 107.550, 107.550, 144.800, 90.00, 90.00, 90.00
R / Rfree (%) 28.2 / 32.1

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half in A "His-on" Conformation (pdb code 3iv9). 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 Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half in A "His-on" Conformation, PDB code: 3iv9:

Cobalt binding site 1 out of 1 in 3iv9

Go back to Cobalt Binding Sites List in 3iv9
Cobalt binding site 1 out of 1 in the Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half in A "His-on" Conformation


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half in A "His-on" Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co1301

b:0.2
occ:1.00
 CO A:B121301 0.0 0.2 1.0
N21 A:B121301 1.9 0.5 1.0
N23 A:B121301 2.0 0.8 1.0
N22 A:B121301 2.0 0.7 1.0
N24 A:B121301 2.0 1.0 1.0
O A:HOH1400 2.1 0.0 1.0
C19 A:B121301 2.9 0.9 1.0
C9 A:B121301 2.9 0.1 1.0
C11 A:B121301 2.9 0.0 1.0
C1 A:B121301 2.9 0.8 1.0
C4 A:B121301 3.0 0.7 1.0
C14 A:B121301 3.1 1.0 1.0
C6 A:B121301 3.1 0.6 1.0
C16 A:B121301 3.1 0.5 1.0
C10 A:B121301 3.2 0.7 1.0
NE2 A:HIS759 3.2 0.5 1.0
C20 A:B121301 3.4 0.7 1.0
C5 A:B121301 3.5 0.4 1.0
C15 A:B121301 3.6 0.8 1.0
CD2 A:HIS759 4.1 0.9 1.0
C18 A:B121301 4.2 0.4 1.0
CE1 A:HIS759 4.2 0.7 1.0
C8 A:B121301 4.2 0.9 1.0
C2 A:B121301 4.3 0.6 1.0
C12 A:B121301 4.3 0.9 1.0
C13 A:B121301 4.3 1.0 1.0
C17 A:B121301 4.3 0.8 1.0
C3 A:B121301 4.3 0.1 1.0
C7 A:B121301 4.4 0.5 1.0
C48 A:B121301 4.8 0.9 1.0
C41 A:B121301 4.8 0.1 1.0
C35 A:B121301 4.9 0.7 1.0
C26 A:B121301 5.0 0.2 1.0

Reference:

M.Koutmos, S.Datta, K.A.Pattridge, J.L.Smith, R.G.Matthews. Insights Into the Reactivation of Cobalamin-Dependent Methionine Synthase. Proc.Natl.Acad.Sci.Usa V. 106 18527 2009.
ISSN: ISSN 0027-8424
PubMed: 19846791
DOI: 10.1073/PNAS.0906132106
Page generated: Sun Jul 13 19:02:08 2025

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