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Atomistry » Zinc » PDB 1f6u-1fp0 » 1foo | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1f6u-1fp0 » 1foo » |
Zinc in PDB 1foo: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free)Enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free)
All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free):
1.14.13.39; Protein crystallography data
The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free), PDB code: 1foo
was solved by
C.S.Raman,
H.Li,
P.Martasek,
B.S.S.Masters,
T.L.Poulos,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1foo:
The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free) also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free)
(pdb code 1foo). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free), PDB code: 1foo: Zinc binding site 1 out of 1 in 1fooGo back to Zinc Binding Sites List in 1foo
Zinc binding site 1 out
of 1 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free)
Mono view Stereo pair view
Reference:
H.Li,
C.S.Raman,
P.Martasek,
B.S.Masters,
T.L.Poulos.
Crystallographic Studies on Endothelial Nitric Oxide Synthase Complexed with Nitric Oxide and Mechanism-Based Inhibitors. Biochemistry V. 40 5399 2001.
Page generated: Sun Oct 13 01:04:14 2024
ISSN: ISSN 0006-2960 PubMed: 11331003 DOI: 10.1021/BI002658V |
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