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Atomistry » Cadmium » PDB 1mws-1qvf » 1q8a » |
Cadmium in PDB 1q8a: Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima (CD2+:L-Hcy Complex, Se-Met)Enzymatic activity of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima (CD2+:L-Hcy Complex, Se-Met)
All present enzymatic activity of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima (CD2+:L-Hcy Complex, Se-Met):
2.1.1.13; Protein crystallography data
The structure of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima (CD2+:L-Hcy Complex, Se-Met), PDB code: 1q8a
was solved by
J.C.Evans,
D.P.Huddler,
M.T.Hilgers,
G.Romanchuk,
R.G.Matthews,
M.L.Ludwig,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Cadmium Binding Sites:
The binding sites of Cadmium atom in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima (CD2+:L-Hcy Complex, Se-Met)
(pdb code 1q8a). This binding sites where shown within
5.0 Angstroms radius around Cadmium atom.
In total 2 binding sites of Cadmium where determined in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima (CD2+:L-Hcy Complex, Se-Met), PDB code: 1q8a: Jump to Cadmium binding site number: 1; 2; Cadmium binding site 1 out of 2 in 1q8aGo back to Cadmium Binding Sites List in 1q8a
Cadmium binding site 1 out
of 2 in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima (CD2+:L-Hcy Complex, Se-Met)
Mono view Stereo pair view
Cadmium binding site 2 out of 2 in 1q8aGo back to Cadmium Binding Sites List in 1q8a
Cadmium binding site 2 out
of 2 in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima (CD2+:L-Hcy Complex, Se-Met)
Mono view Stereo pair view
Reference:
J.C.Evans,
D.P.Huddler,
M.T.Hilgers,
G.Romanchuk,
R.G.Matthews,
M.L.Ludwig.
Structures of the N-Terminal Modules Imply Large Domain Motions During Catalysis By Methionine Synthase. Proc.Natl.Acad.Sci.Usa V. 101 3729 2004.
Page generated: Fri Jul 19 14:08:28 2024
ISSN: ISSN 0027-8424 PubMed: 14752199 DOI: 10.1073/PNAS.0308082100 |
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