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Atomistry » Iron » PDB 8wqx-9f6l » 9eqf | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Iron » PDB 8wqx-9f6l » 9eqf » |
Iron in PDB 9eqf: Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and SuccinateEnzymatic activity of Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate
All present enzymatic activity of Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate:
1.14.11.41; Protein crystallography data
The structure of Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate, PDB code: 9eqf
was solved by
F.J.Hardy,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate
(pdb code 9eqf). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate, PDB code: 9eqf: Iron binding site 1 out of 1 in 9eqfGo back to Iron Binding Sites List in 9eqf
Iron binding site 1 out
of 1 in the Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate
Mono view Stereo pair view
Reference:
F.J.Hardy,
M.G.Quesne,
E.F.Gerard,
J.Zhao,
M.Ortmayer,
C.J.Taylor,
H.S.Ali,
J.W.Slater,
C.W.Levy,
D.J.Heyes,
J.M.J.Bollinger,
S.P.De Visser,
A.P.Green.
Probing Ferryl Reactivity in A Nonheme Iron Oxygenase Using An Expanded Genetic Code Acs Catalysis 11584 2024.
Page generated: Sun Aug 11 12:05:45 2024
ISSN: ESSN 2155-5435 DOI: 10.1021/ACSCATAL.4C02365 |
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