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Atomistry » Chlorine » PDB 1nvf-1o3m » 1nzv | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 1nvf-1o3m » 1nzv » |
Chlorine in PDB 1nzv: Crystal Structure of Src SH2 Domain Bound to Doubly Phosphorylated Peptide PqpyipyvpaEnzymatic activity of Crystal Structure of Src SH2 Domain Bound to Doubly Phosphorylated Peptide Pqpyipyvpa
All present enzymatic activity of Crystal Structure of Src SH2 Domain Bound to Doubly Phosphorylated Peptide Pqpyipyvpa:
2.7.1.112; Protein crystallography data
The structure of Crystal Structure of Src SH2 Domain Bound to Doubly Phosphorylated Peptide Pqpyipyvpa, PDB code: 1nzv
was solved by
O.Y.Lubman,
G.Waksman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Src SH2 Domain Bound to Doubly Phosphorylated Peptide Pqpyipyvpa
(pdb code 1nzv). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Src SH2 Domain Bound to Doubly Phosphorylated Peptide Pqpyipyvpa, PDB code: 1nzv: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 1nzvGo back to Chlorine Binding Sites List in 1nzv
Chlorine binding site 1 out
of 2 in the Crystal Structure of Src SH2 Domain Bound to Doubly Phosphorylated Peptide Pqpyipyvpa
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 1nzvGo back to Chlorine Binding Sites List in 1nzv
Chlorine binding site 2 out
of 2 in the Crystal Structure of Src SH2 Domain Bound to Doubly Phosphorylated Peptide Pqpyipyvpa
Mono view Stereo pair view
Reference:
O.Y.Lubman,
G.Waksman.
Structural and Thermodynamic Basis For the Interaction of the Src SH2 Domain with the Activated Form of the Pdgf Beta-Receptor J.Mol.Biol. V. 328 655 2003.
Page generated: Sat Dec 12 08:44:13 2020
ISSN: ISSN 0022-2836 PubMed: 12706723 DOI: 10.1016/S0022-2836(03)00344-9 |
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