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Atomistry » Zinc » PDB 3e2d-3eb5 » 3eah | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3e2d-3eb5 » 3eah » |
Zinc in PDB 3eah: Structure of Inhibited Human Enos Oxygenase DomainEnzymatic activity of Structure of Inhibited Human Enos Oxygenase Domain
All present enzymatic activity of Structure of Inhibited Human Enos Oxygenase Domain:
1.14.13.39; Protein crystallography data
The structure of Structure of Inhibited Human Enos Oxygenase Domain, PDB code: 3eah
was solved by
E.D.Garcin,
A.S.Arvai,
R.J.Rosenfeld,
M.D.Kroeger,
B.R.Crane,
G.Andersson,
G.Andrews,
P.J.Hamley,
P.R.Mallinder,
D.J.Nicholls,
S.A.St-Gallay,
A.C.Tinker,
N.P.Gensmantel,
A.Mete,
D.R.Cheshire,
S.Connolly,
D.J.Stuehr,
A.Aberg,
A.V.Wallace,
J.A.Tainer,
E.D.Getzoff,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3eah:
The structure of Structure of Inhibited Human Enos Oxygenase Domain also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Inhibited Human Enos Oxygenase Domain
(pdb code 3eah). 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 Structure of Inhibited Human Enos Oxygenase Domain, PDB code: 3eah: Zinc binding site 1 out of 1 in 3eahGo back to Zinc Binding Sites List in 3eah
Zinc binding site 1 out
of 1 in the Structure of Inhibited Human Enos Oxygenase Domain
Mono view Stereo pair view
Reference:
E.D.Garcin,
A.S.Arvai,
R.J.Rosenfeld,
M.D.Kroeger,
B.R.Crane,
G.Andersson,
G.Andrews,
P.J.Hamley,
P.R.Mallinder,
D.J.Nicholls,
S.A.St-Gallay,
A.C.Tinker,
N.P.Gensmantel,
A.Mete,
D.R.Cheshire,
S.Connolly,
D.J.Stuehr,
A.Aberg,
A.V.Wallace,
J.A.Tainer,
E.D.Getzoff.
Anchored Plasticity Opens Doors For Selective Inhibitor Design in Nitric Oxide Synthase. Nat.Chem.Biol. V. 4 700 2008.
Page generated: Wed Dec 16 04:15:22 2020
ISSN: ISSN 1552-4450 PubMed: 18849972 DOI: 10.1038/NCHEMBIO.115 |
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