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PDBsum entry 3nqs
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Oxidoreductase
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PDB id
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3nqs
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Oxidoreductase
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Title:
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Crystal structure of inducible nitric oxide synthase with n- nitrosated-pterin
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Structure:
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Nitric oxide synthase, inducible. Chain: a, b. Fragment: unp residues 66-498. Synonym: inducible no synthase, inducible nos, inos, nos type ii, macrophage nos, mac-nos. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Strain: macrophage. Gene: inosl, nos2. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.20Å
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R-factor:
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0.204
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R-free:
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0.229
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Authors:
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R.J.Rosenfeld,E.D.Getzoff,J.A.Tainer
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Key ref:
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R.J.Rosenfeld
et al.
(2010).
Nitric-oxide synthase forms N-NO-pterin and S-NO-cys: implications for activity, allostery, and regulation.
J Biol Chem,
285,
31581-31589.
PubMed id:
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Date:
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29-Jun-10
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Release date:
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21-Jul-10
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PROCHECK
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Headers
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References
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P29477
(NOS2_MOUSE) -
Nitric oxide synthase, inducible from Mus musculus
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Seq: Struc:
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1144 a.a.
413 a.a.
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Key: |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.1.14.13.39
- nitric-oxide synthase (NADPH).
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Reaction:
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2 L-arginine + 3 NADPH + 4 O2 + H+ = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
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2
×
L-arginine
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+
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3
×
NADPH
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+
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4
×
O2
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+
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H(+)
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=
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2
×
L-citrulline
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+
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2
×
nitric oxide
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+
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3
×
NADP(+)
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+
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4
×
H2O
Bound ligand (Het Group name = )
corresponds exactly
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Biol Chem
285:31581-31589
(2010)
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PubMed id:
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Nitric-oxide synthase forms N-NO-pterin and S-NO-cys: implications for activity, allostery, and regulation.
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R.J.Rosenfeld,
J.Bonaventura,
B.R.Szymczyna,
M.J.MacCoss,
A.S.Arvai,
J.R.Yates,
J.A.Tainer,
E.D.Getzoff.
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ABSTRACT
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');
}
}
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