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Atomistry » Calcium » PDB 1px7-1qcp » 1qco » |
Calcium in PDB 1qco: Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and AcetoacetateEnzymatic activity of Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate
All present enzymatic activity of Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate:
3.7.1.2; Protein crystallography data
The structure of Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate, PDB code: 1qco
was solved by
D.E.Timm,
H.A.Mueller,
P.Bhanumoorthy,
J.M.Harp,
G.J.Bunick,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1qco:
The structure of Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate
(pdb code 1qco). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate, PDB code: 1qco: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 1qcoGo back to Calcium Binding Sites List in 1qco
Calcium binding site 1 out
of 2 in the Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 1qcoGo back to Calcium Binding Sites List in 1qco
Calcium binding site 2 out
of 2 in the Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate
Mono view Stereo pair view
Reference:
D.E.Timm,
H.A.Mueller,
P.Bhanumoorthy,
J.M.Harp,
G.J.Bunick.
Crystal Structure and Mechanism of A Carbon-Carbon Bond Hydrolase. Structure Fold.Des. V. 7 1023 1999.
Page generated: Sat Dec 12 03:16:09 2020
ISSN: ISSN 0969-2126 PubMed: 10508789 DOI: 10.1016/S0969-2126(99)80170-1 |
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