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Atomistry » Arsenic » PDB 1q2o-1yhc » 1qqj » |
Arsenic in PDB 1qqj: Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom ResolutionEnzymatic activity of Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution
All present enzymatic activity of Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution:
3.7.1.2; Protein crystallography data
The structure of Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution, PDB code: 1qqj
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 1qqj:
The structure of Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution also contains other interesting chemical elements:
Arsenic Binding Sites:
The binding sites of Arsenic atom in the Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution
(pdb code 1qqj). This binding sites where shown within
5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution, PDB code: 1qqj: Jump to Arsenic binding site number: 1; 2; Arsenic binding site 1 out of 2 in 1qqjGo back to![]() ![]()
Arsenic binding site 1 out
of 2 in the Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution
![]() Mono view ![]() Stereo pair view
Arsenic binding site 2 out of 2 in 1qqjGo back to![]() ![]()
Arsenic binding site 2 out
of 2 in the Crystal Structure of Mouse Fumarylacetoacetate Hydrolase Refined at 1.55 Angstrom Resolution
![]() 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: Sun Jul 6 23:00:09 2025
ISSN: ISSN 0969-2126 PubMed: 10508789 DOI: 10.1016/S0969-2126(99)80170-1 |
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