4nos | pdb_00004nos
HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE WITH INHIBITOR
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| 4nos, resolution 2.250Å | |||||||||||||
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| Ligands: | H2B, H4B, HEM, ITU, ZN | ||||||||||||
| Activity: | Nitric-oxide synthase, with EC number 1.14.13.39 | ||||||||||||
| Related: | 3NOS
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.
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
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