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Atomistry » Zinc » PDB 1cp6-1d4u » 1d1w | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1cp6-1d4u » 1d1w » |
Zinc in PDB 1d1w: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound)Enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound)
All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound):
1.14.13.39; Protein crystallography data
The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound), PDB code: 1d1w
was solved by
H.Li,
C.S.Raman,
P.Martasek,
V.Kral,
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 1d1w:
The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound) 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 2- Aminothiazoline (H4B Bound)
(pdb code 1d1w). 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 2- Aminothiazoline (H4B Bound), PDB code: 1d1w: Zinc binding site 1 out of 1 in 1d1wGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 2- Aminothiazoline (H4B Bound)
![]() Mono view ![]() Stereo pair view
Reference:
H.Li,
C.S.Raman,
P.Martasek,
V.Kral,
B.S.Masters,
T.L.Poulos.
Mapping the Active Site Polarity in Structures of Endothelial Nitric Oxide Synthase Heme Domain Complexed with Isothioureas. J.Inorg.Biochem. V. 81 133 2000.
Page generated: Sat Oct 12 23:27:00 2024
ISSN: ISSN 0162-0134 PubMed: 11051558 DOI: 10.1016/S0162-0134(00)00099-4 |
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