1aye: Difference between revisions
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|PDB= 1aye |SIZE=350|CAPTION= <scene name='initialview01'>1aye</scene>, resolution 1.8Å | |PDB= 1aye |SIZE=350|CAPTION= <scene name='initialview01'>1aye</scene>, resolution 1.8Å | ||
|SITE= <scene name='pdbsite=1:Subsite+S1'+ARG+145,+ASN+144,+TYR+248+Subsite+S1+ARG+127+...'>1</scene> | |SITE= <scene name='pdbsite=1:Subsite+S1'+ARG+145,+ASN+144,+TYR+248+Subsite+S1+ARG+127+...'>1</scene> | ||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Carboxypeptidase_A2 Carboxypeptidase A2], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.15 3.4.17.15] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxypeptidase_A2 Carboxypeptidase A2], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.15 3.4.17.15] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aye OCA], [http://www.ebi.ac.uk/pdbsum/1aye PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aye RCSB]</span> | |||
}} | }} | ||
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[[Category: Reverte, D.]] | [[Category: Reverte, D.]] | ||
[[Category: Vendrell, J.]] | [[Category: Vendrell, J.]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
[[Category: zymogen]] | [[Category: zymogen]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:49:55 2008'' | ||
Revision as of 18:50, 30 March 2008
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| , resolution 1.8Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Carboxypeptidase A2, with EC number 3.4.17.15 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN PROCARBOXYPEPTIDASE A2
OverviewOverview
The three-dimensional structure of human procarboxypeptidase A2 has been determined using X-ray crystallography at 1.8 A resolution. This is the first detailed structural report of a human pancreatic carboxypeptidase and of its zymogen. Human procarboxypeptidase A2 is formed by a pro-segment of 96 residues, which inhibits the enzyme, and a carboxypeptidase moiety of 305 residues. The pro-enzyme maintains the general fold when compared with other non-human counterparts. The globular part of the pro-segment docks into the enzyme moiety and shields the S2-S4 substrate binding sites, promoting inhibition. Interestingly, important differences are found in the pro-segment which allow the identification of the structural determinants of the diverse activation behaviours of procarboxypeptidases A1, B and A2, particularly of the latter. The benzylsuccinic inhibitor is able to diffuse into the active site of procarboxypeptidase A2 in the crystals. The structure of the zymogen-inhibitor complex has been solved at 2.2 A resolution. The inhibitor enters the active site through a channel formed at the interface between the pro-segment and the enzyme regions and interacts with important elements of the active site. The derived structural features explain the intrinsic activity of A1/A2 pro-enzymes for small substrates.
About this StructureAbout this Structure
1AYE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen., Garcia-Saez I, Reverter D, Vendrell J, Aviles FX, Coll M, EMBO J. 1997 Dec 1;16(23):6906-13. PMID:9384570
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