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Calcium in PDB 6q6j: Human Phosphoserine Phosphatase with Substrate Analogue Homo-Cysteic AcidEnzymatic activity of Human Phosphoserine Phosphatase with Substrate Analogue Homo-Cysteic Acid
All present enzymatic activity of Human Phosphoserine Phosphatase with Substrate Analogue Homo-Cysteic Acid:
3.1.3.3; Protein crystallography data
The structure of Human Phosphoserine Phosphatase with Substrate Analogue Homo-Cysteic Acid, PDB code: 6q6j
was solved by
J.Wouters,
M.Haufroid,
M.Mirgaux,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6q6j:
The structure of Human Phosphoserine Phosphatase with Substrate Analogue Homo-Cysteic Acid also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Human Phosphoserine Phosphatase with Substrate Analogue Homo-Cysteic Acid
(pdb code 6q6j). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Human Phosphoserine Phosphatase with Substrate Analogue Homo-Cysteic Acid, PDB code: 6q6j: Jump to Calcium binding site number: 1; 2; 3; Calcium binding site 1 out of 3 in 6q6jGo back to Calcium Binding Sites List in 6q6j
Calcium binding site 1 out
of 3 in the Human Phosphoserine Phosphatase with Substrate Analogue Homo-Cysteic Acid
Mono view Stereo pair view
Calcium binding site 2 out of 3 in 6q6jGo back to Calcium Binding Sites List in 6q6j
Calcium binding site 2 out
of 3 in the Human Phosphoserine Phosphatase with Substrate Analogue Homo-Cysteic Acid
Mono view Stereo pair view
Calcium binding site 3 out of 3 in 6q6jGo back to Calcium Binding Sites List in 6q6j
Calcium binding site 3 out
of 3 in the Human Phosphoserine Phosphatase with Substrate Analogue Homo-Cysteic Acid
Mono view Stereo pair view
Reference:
M.Haufroid,
M.Mirgaux,
L.Leherte,
J.Wouters.
Crystal Structures and Snapshots Along the Reaction Pathway of Human Phosphoserine Phosphatase. Acta Crystallogr D Struct V. 75 592 2019BIOL.
Page generated: Sat Dec 12 07:26:57 2020
ISSN: ISSN 2059-7983 PubMed: 31205021 DOI: 10.1107/S2059798319006867 |
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