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Atomistry » Calcium » PDB 3bxl-3cfw » 3bxm » |
Calcium in PDB 3bxm: Structure of An Inactive Mutant of Human Glutamate Carboxypeptidase II [Gcpii(E424A)] in Complex with N-Acetyl-Asp-Glu (Naag)Enzymatic activity of Structure of An Inactive Mutant of Human Glutamate Carboxypeptidase II [Gcpii(E424A)] in Complex with N-Acetyl-Asp-Glu (Naag)
All present enzymatic activity of Structure of An Inactive Mutant of Human Glutamate Carboxypeptidase II [Gcpii(E424A)] in Complex with N-Acetyl-Asp-Glu (Naag):
3.4.17.21; Protein crystallography data
The structure of Structure of An Inactive Mutant of Human Glutamate Carboxypeptidase II [Gcpii(E424A)] in Complex with N-Acetyl-Asp-Glu (Naag), PDB code: 3bxm
was solved by
J.Lubkowski,
C.Barinka,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3bxm:
The structure of Structure of An Inactive Mutant of Human Glutamate Carboxypeptidase II [Gcpii(E424A)] in Complex with N-Acetyl-Asp-Glu (Naag) also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Structure of An Inactive Mutant of Human Glutamate Carboxypeptidase II [Gcpii(E424A)] in Complex with N-Acetyl-Asp-Glu (Naag)
(pdb code 3bxm). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of An Inactive Mutant of Human Glutamate Carboxypeptidase II [Gcpii(E424A)] in Complex with N-Acetyl-Asp-Glu (Naag), PDB code: 3bxm: Calcium binding site 1 out of 1 in 3bxmGo back to Calcium Binding Sites List in 3bxm
Calcium binding site 1 out
of 1 in the Structure of An Inactive Mutant of Human Glutamate Carboxypeptidase II [Gcpii(E424A)] in Complex with N-Acetyl-Asp-Glu (Naag)
Mono view Stereo pair view
Reference:
V.Klusak,
C.Barinka,
A.Plechanovova,
P.Mlcochova,
J.Konvalinka,
L.Rulisek,
J.Lubkowski.
Reaction Mechanism of Glutamate Carboxypeptidase II Revealed By Mutagenesis, X-Ray Crystallography, and Computational Methods. Biochemistry V. 48 4126 2009.
Page generated: Sat Jul 13 08:29:42 2024
ISSN: ISSN 0006-2960 PubMed: 19301871 DOI: 10.1021/BI900220S |
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