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Cobalt in PDB 3iva: Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half with Adohcy Bound

Enzymatic activity of Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half with Adohcy Bound

All present enzymatic activity of Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half with Adohcy Bound:
2.1.1.13;

Protein crystallography data

The structure of Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half with Adohcy Bound, PDB code: 3iva 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) 45.32 / 2.70
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 107.006, 107.006, 141.185, 90.00, 90.00, 90.00
R / Rfree (%) 24.6 / 30

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half with Adohcy Bound (pdb code 3iva). 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 with Adohcy Bound, PDB code: 3iva:

Cobalt binding site 1 out of 1 in 3iva

Go back to Cobalt Binding Sites List in 3iva
Cobalt binding site 1 out of 1 in the Structure of the B12-Dependent Methionine Synthase (Meth) C-Teminal Half with Adohcy Bound


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 with Adohcy Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co1301

b:73.3
occ:1.00
 CO A:B121301 0.0 73.3 1.0
N22 A:B121301 1.9 69.9 1.0
N21 A:B121301 1.9 73.0 1.0
N24 A:B121301 2.0 79.8 1.0
N23 A:B121301 2.0 77.1 1.0
C9 A:B121301 2.8 70.5 1.0
C11 A:B121301 2.9 75.8 1.0
C19 A:B121301 2.9 78.0 1.0
C1 A:B121301 3.0 75.6 1.0
C10 A:B121301 3.0 74.2 1.0
C4 A:B121301 3.1 72.3 1.0
C14 A:B121301 3.1 78.8 1.0
C16 A:B121301 3.1 81.8 1.0
C6 A:B121301 3.1 69.0 1.0
C20 A:B121301 3.4 75.5 1.0
C5 A:B121301 3.5 70.7 1.0
C15 A:B121301 3.5 81.5 1.0
O A:HOH1310 3.9 61.8 1.0
OH A:TYR1139 4.0 48.4 1.0
C8 A:B121301 4.2 67.0 1.0
C18 A:B121301 4.2 82.3 1.0
C12 A:B121301 4.3 77.0 1.0
C13 A:B121301 4.3 78.9 1.0
C2 A:B121301 4.3 75.0 1.0
C7 A:B121301 4.3 67.4 1.0
C3 A:B121301 4.4 74.4 1.0
C17 A:B121301 4.4 84.1 1.0
CE2 A:TYR1139 4.6 47.2 1.0
CZ A:TYR1139 4.7 48.7 1.0
C41 A:B121301 4.8 67.6 1.0
CD2 A:LEU806 4.9 70.8 1.0
C53 A:B121301 4.9 83.9 1.0
C37 A:B121301 4.9 65.7 1.0
C26 A:B121301 4.9 74.7 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 19:02:22 2025

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