1foo: Difference between revisions
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|PDB= 1foo |SIZE=350|CAPTION= <scene name='initialview01'>1foo</scene>, resolution 2.00Å | |PDB= 1foo |SIZE=350|CAPTION= <scene name='initialview01'>1foo</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITROGEN+OXIDE'>NO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </span> | |||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[4nse|4NSE]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1foo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1foo OCA], [http://www.ebi.ac.uk/pdbsum/1foo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1foo RCSB]</span> | |||
}} | }} | ||
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[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||
[[Category: Raman, C S.]] | [[Category: Raman, C S.]] | ||
[[Category: alpha-beta fold]] | [[Category: alpha-beta fold]] | ||
[[Category: nitric oxide synthase]] | [[Category: nitric oxide synthase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:27:06 2008'' | ||
Revision as of 20:27, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | , , , , , , | ||||||
| Activity: | Nitric-oxide synthase, with EC number 1.14.13.39 | ||||||
| Related: | 4NSE
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG AND NO(H4B-FREE)
OverviewOverview
The crystal structure of the endothelial nitric oxide synthase (NOS) heme domain complexed with NO reveals close hydrogen bonding interactions between NO and the terminal guanidino nitrogen of the substrate, L-arginine. Dioxygen is expected to bind in a similar mode which will facilitate proton abstraction from L-Arg to dioxygen, a required step for O-O bond cleavage. Structures of mechanism-based NOS inhibitors, N(5)-(1-iminoethyl)-L-ornithine and N-(3-(aminomethyl)benzyl)acetamidine, provide clues on how this class of compounds operate as suicide substrate inhibitors leading to heme oxidation.
About this StructureAbout this Structure
1FOO is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors., Li H, Raman CS, Martasek P, Masters BS, Poulos TL, Biochemistry. 2001 May 8;40(18):5399-406. PMID:11331003
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