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Atomistry » Iron » PDB 1nml-1o1i » 1noc » |
Iron in PDB 1noc: Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114) Complexed with Type I E. Coli Chloramphenicol Acetyl Transferase and ImidazoleEnzymatic activity of Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114) Complexed with Type I E. Coli Chloramphenicol Acetyl Transferase and Imidazole
All present enzymatic activity of Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114) Complexed with Type I E. Coli Chloramphenicol Acetyl Transferase and Imidazole:
1.14.13.39; 2.3.1.28; Protein crystallography data
The structure of Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114) Complexed with Type I E. Coli Chloramphenicol Acetyl Transferase and Imidazole, PDB code: 1noc
was solved by
B.R.Crane,
A.S.Arvai,
E.D.Getzoff,
D.J.Stuehr,
J.A.Tainer,
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 Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114) Complexed with Type I E. Coli Chloramphenicol Acetyl Transferase and Imidazole
(pdb code 1noc). 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 Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114) Complexed with Type I E. Coli Chloramphenicol Acetyl Transferase and Imidazole, PDB code: 1noc: Iron binding site 1 out of 1 in 1nocGo back to![]() ![]()
Iron binding site 1 out
of 1 in the Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114) Complexed with Type I E. Coli Chloramphenicol Acetyl Transferase and Imidazole
![]() Mono view ![]() Stereo pair view
Reference:
B.R.Crane,
A.S.Arvai,
R.Gachhui,
C.Wu,
D.K.Ghosh,
E.D.Getzoff,
D.J.Stuehr,
J.A.Tainer.
The Structure of Nitric Oxide Synthase Oxygenase Domain and Inhibitor Complexes. Science V. 278 425 1997.
Page generated: Sat Aug 3 11:57:18 2024
ISSN: ISSN 0036-8075 PubMed: 9334294 DOI: 10.1126/SCIENCE.278.5337.425 |
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