1afq
From Proteopedia
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|PDB= 1afq |SIZE=350|CAPTION= <scene name='initialview01'>1afq</scene>, resolution 1.80Å | |PDB= 1afq |SIZE=350|CAPTION= <scene name='initialview01'>1afq</scene>, resolution 1.80Å | ||
|SITE= <scene name='pdbsite=CAT:Catalytic+Triad'>CAT</scene> | |SITE= <scene name='pdbsite=CAT:Catalytic+Triad'>CAT</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=FBA:4-FLUOROBENZYLAMINE'>FBA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1afq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1afq OCA], [http://www.ebi.ac.uk/pdbsum/1afq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1afq RCSB]</span> | ||
}} | }} | ||
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[[Category: Shimohigashi, Y.]] | [[Category: Shimohigashi, Y.]] | ||
[[Category: Sugio, S.]] | [[Category: Sugio, S.]] | ||
| - | [[Category: SO4]] | ||
[[Category: complex (serine protease/inhibitor)]] | [[Category: complex (serine protease/inhibitor)]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''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 18:39:12 2008'' |
Revision as of 15:39, 30 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Chymotrypsin, with EC number 3.4.21.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF BOVINE GAMMA-CHYMOTRYPSIN COMPLEXED WITH A SYNTHETIC INHIBITOR
Overview
Crystals of gamma-chymotrypsin grown in aqueous solution were soaked in n-hexane, and the structures of both the soaked and the native crystals were determined to 2.2-A resolution. Seven hexane molecules and 130 water molecules were found in the hexane-soaked crystals. Two of the seven hexane molecules are found near the active site, and the rest are close to hydrophobic regions on or near the surface of the enzyme. In the hexane structure, water molecules that were not observed in the native structure form a clathrate around one of the hexane molecules. Only 97 water molecules were found in the native structure. The temperature factors for atoms in the hexane environment are lower than those in the aqueous environment. There are significant changes between the two structures in the side chains of both polar and neutral residues, particularly in the vicinity of the hexane molecules. These changes have perturbed the hydrogen-bonding patterns. The electron density for the peptide bound in the active site has been dramatically altered in hexane and appears to be tetrahedral at the carbon that is covalently bound to Ser 195. The crystalline enzyme retains its active conformation in the nonpolar medium and can catalyze both hydrolysis and synthesis reactions in hexane.
About this Structure
1AFQ is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of gamma-chymotrypsin in hexane., Yennawar NH, Yennawar HP, Farber GK, Biochemistry. 1994 Jun 14;33(23):7326-36. PMID:8003497
Page seeded by OCA on Sun Mar 30 18:39:12 2008
