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Atomistry » Calcium » PDB 4m93-4mpp » 4mcs » |
Calcium in PDB 4mcs: A High Resolution Structure of Human Glutamate Carboxypeptidase II (Gcpii) HIS475TYR Variant in Complex with Glutamic AcidEnzymatic activity of A High Resolution Structure of Human Glutamate Carboxypeptidase II (Gcpii) HIS475TYR Variant in Complex with Glutamic Acid
All present enzymatic activity of A High Resolution Structure of Human Glutamate Carboxypeptidase II (Gcpii) HIS475TYR Variant in Complex with Glutamic Acid:
3.4.17.21; Protein crystallography data
The structure of A High Resolution Structure of Human Glutamate Carboxypeptidase II (Gcpii) HIS475TYR Variant in Complex with Glutamic Acid, PDB code: 4mcs
was solved by
J.Ptacek,
C.Barinka,
P.Sacha,
M.Navratil,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4mcs:
The structure of A High Resolution Structure of Human Glutamate Carboxypeptidase II (Gcpii) HIS475TYR Variant in Complex with Glutamic Acid also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the A High Resolution Structure of Human Glutamate Carboxypeptidase II (Gcpii) HIS475TYR Variant in Complex with Glutamic Acid
(pdb code 4mcs). 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 A High Resolution Structure of Human Glutamate Carboxypeptidase II (Gcpii) HIS475TYR Variant in Complex with Glutamic Acid, PDB code: 4mcs: Calcium binding site 1 out of 1 in 4mcsGo back to Calcium Binding Sites List in 4mcs
Calcium binding site 1 out
of 1 in the A High Resolution Structure of Human Glutamate Carboxypeptidase II (Gcpii) HIS475TYR Variant in Complex with Glutamic Acid
Mono view Stereo pair view
Reference:
M.Navratil,
J.Ptacek,
P.Sacha,
J.Starkova,
J.Lubkowski,
C.Barinka,
J.Konvalinka.
Structural and Biochemical Characterization of the Folyl-Poly-Gamma-L-Glutamate Hydrolyzing Activity of Human Glutamate Carboxypeptidase II. Febs J. V. 281 3228 2014.
Page generated: Sat Dec 12 04:58:43 2020
ISSN: ISSN 1742-464X PubMed: 24863754 DOI: 10.1111/FEBS.12857 |
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