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Atomistry » Cadmium » PDB 2eil-2mhu » 2hcr » |
Cadmium in PDB 2hcr: Crystal Structure of Human Phosphoribosyl Pyrophosphate Synthetase 1 in Complex with Amp(Atp), Cadmium and Sulfate IonEnzymatic activity of Crystal Structure of Human Phosphoribosyl Pyrophosphate Synthetase 1 in Complex with Amp(Atp), Cadmium and Sulfate Ion
All present enzymatic activity of Crystal Structure of Human Phosphoribosyl Pyrophosphate Synthetase 1 in Complex with Amp(Atp), Cadmium and Sulfate Ion:
2.7.6.1; Protein crystallography data
The structure of Crystal Structure of Human Phosphoribosyl Pyrophosphate Synthetase 1 in Complex with Amp(Atp), Cadmium and Sulfate Ion, PDB code: 2hcr
was solved by
S.Li,
B.Peng,
J.Ding,
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 Crystal Structure of Human Phosphoribosyl Pyrophosphate Synthetase 1 in Complex with Amp(Atp), Cadmium and Sulfate Ion
(pdb code 2hcr). This binding sites where shown within
5.0 Angstroms radius around Cadmium atom.
In total 2 binding sites of Cadmium where determined in the Crystal Structure of Human Phosphoribosyl Pyrophosphate Synthetase 1 in Complex with Amp(Atp), Cadmium and Sulfate Ion, PDB code: 2hcr: Jump to Cadmium binding site number: 1; 2; Cadmium binding site 1 out of 2 in 2hcrGo back to![]() ![]()
Cadmium binding site 1 out
of 2 in the Crystal Structure of Human Phosphoribosyl Pyrophosphate Synthetase 1 in Complex with Amp(Atp), Cadmium and Sulfate Ion
![]() Mono view ![]() Stereo pair view
Cadmium binding site 2 out of 2 in 2hcrGo back to![]() ![]()
Cadmium binding site 2 out
of 2 in the Crystal Structure of Human Phosphoribosyl Pyrophosphate Synthetase 1 in Complex with Amp(Atp), Cadmium and Sulfate Ion
![]() Mono view ![]() Stereo pair view
Reference:
S.Li,
Y.Lu,
B.Peng,
J.Ding.
Crystal Structure of Human Phosphoribosylpyrophosphate Synthetase 1 Reveals A Novel Allosteric Site Biochem.J. V. 401 39 2007.
Page generated: Thu Jul 10 11:53:00 2025
ISSN: ISSN 0264-6021 PubMed: 16939420 DOI: 10.1042/BJ20061066 |
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