1d1w
From Proteopedia
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|PDB= 1d1w |SIZE=350|CAPTION= <scene name='initialview01'>1d1w</scene>, resolution 2.00Å | |PDB= 1d1w |SIZE=350|CAPTION= <scene name='initialview01'>1d1w</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATQ:2-AMINOTHIAZOLINE'>ATQ</scene>, <scene name='pdbligand=CAD:CACODYLIC+ACID'>CAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [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] | + | |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=[[1nse|1NSE]], [[1d0c|1D0C]], [[1d0o|1D0O]], [[1d0p|1D0P]], [[1d1v|1D1V]], [[1d1w|1D1W]], [[1d1x|1D1X]], [[1d1y|1D1Y]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d1w OCA], [http://www.ebi.ac.uk/pdbsum/1d1w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d1w RCSB]</span> | ||
}} | }} | ||
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[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||
[[Category: Raman, C S.]] | [[Category: Raman, C S.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: ATQ]] | ||
| - | [[Category: CAD]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: H4B]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: ZN]] | ||
[[Category: alpha-beta fold]] | [[Category: alpha-beta fold]] | ||
| - | ''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 19:32:54 2008'' |
Revision as of 16:32, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , | ||||||
| Activity: | Nitric-oxide synthase, with EC number 1.14.13.39 | ||||||
| Related: | 1NSE, 1D0C, 1D0O, 1D0P, 1D1V, 1D1W, 1D1X, 1D1Y
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 2-AMINOTHIAZOLINE (H4B BOUND)
Overview
Analyzing the active site topology and plasticity of nitric oxide synthase (NOS) and understanding enzyme-drug interactions are crucial for the development of potent, isoform-selective NOS inhibitors. A small hydrophobic pocket in the active site is identified in the bovine eNOS heme domain structures complexed with potent isothiourea inhibitors: seleno analogue of S-ethyl-isothiourea, S-isopropyl-isothiourea, and 2-aminothiazoline, respectively. These structures reveal the importance of nonpolar van der Waals contacts in addition to the well-known hydrogen bonding interactions between inhibitor and enzyme. The scaffold of a potent NOS inhibitor should be capable of donating hydrogen bonds to as well as making nonpolar contacts with amino acids in the NOS active site.
About this Structure
1D1W is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas., Li H, Raman CS, Martasek P, Kral V, Masters BS, Poulos TL, J Inorg Biochem. 2000 Aug 31;81(3):133-9. PMID:11051558
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