4nos
From Proteopedia
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| , resolution 2.250Å | |||||||
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| Ligands: | , , , and | ||||||
| Activity: | Nitric-oxide synthase, with EC number 1.14.13.39 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE WITH INHIBITOR
Contents |
Overview
Crystal structures of human endothelial nitric oxide synthase (eNOS) and human inducible NOS (iNOS) catalytic domains were solved in complex with the arginine substrate and an inhibitor S-ethylisothiourea (SEITU), respectively. The small molecules bind in a narrow cleft within the larger active-site cavity containing heme and tetrahydrobiopterin. Both are hydrogen-bonded to a conserved glutamate (eNOS E361, iNOS E377). The active-site residues of iNOS and eNOS are nearly identical. Nevertheless, structural comparisons provide a basis for design of isozyme-selective inhibitors. The high-resolution, refined structures of eNOS (2.4 A resolution) and iNOS (2.25 A resolution) reveal an unexpected structural zinc situated at the intermolecular interface and coordinated by four cysteines, two from each monomer.
Disease
Known diseases associated with this structure: Hypertension, susceptibility to OMIM:[163730], Malaria, resistance to OMIM:[163730]
About this Structure
4NOS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation., Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC, Nat Struct Biol. 1999 Mar;6(3):233-42. PMID:10074942
Page seeded by OCA on Thu Mar 20 19:10:24 2008
Categories: Homo sapiens | Nitric-oxide synthase | Single protein | Fischmann, T O. | Weber, P C. | H2B | H4B | HEM | ITU | ZN | Human | L-arginine monooxygenase | Nitric oxide | Zns4
