1afq
From Proteopedia
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| - | [[Image:1afq.gif|left|200px]]<br /> | + | [[Image:1afq.gif|left|200px]]<br /><applet load="1afq" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1afq" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1afq, resolution 1.80Å" /> | caption="1afq, resolution 1.80Å" /> | ||
'''CRYSTAL STRUCTURE OF BOVINE GAMMA-CHYMOTRYPSIN COMPLEXED WITH A SYNTHETIC INHIBITOR'''<br /> | '''CRYSTAL STRUCTURE OF BOVINE GAMMA-CHYMOTRYPSIN COMPLEXED WITH A SYNTHETIC INHIBITOR'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AFQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] | + | 1AFQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Site: <scene name='pdbsite=CAT:Catalytic Triad'>CAT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AFQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:14:36 2007'' |
Revision as of 12:04, 18 December 2007
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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 with SO4 as ligand. Active as Chymotrypsin, with EC number 3.4.21.1 Known structural/functional Site: . 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
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