Atomistry » Cobalt » PDB 3igz-3mcr » 3iv9
Atomistry »
  Cobalt »
    PDB 3igz-3mcr »
      3iv9 »

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: Tue Jul 30 16:12:08 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy