1ve6
From Proteopedia
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|PDB= 1ve6 |SIZE=350|CAPTION= <scene name='initialview01'>1ve6</scene>, resolution 2.1Å | |PDB= 1ve6 |SIZE=350|CAPTION= <scene name='initialview01'>1ve6</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene> | + | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ve7|1VE7]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ve6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ve6 OCA], [http://www.ebi.ac.uk/pdbsum/1ve6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ve6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Yang, H.]] | [[Category: Yang, H.]] | ||
[[Category: Zhao, X.]] | [[Category: Zhao, X.]] | ||
| - | [[Category: BOG]] | ||
| - | [[Category: GOL]] | ||
[[Category: alpha/beta hydrolase domain]] | [[Category: alpha/beta hydrolase domain]] | ||
[[Category: beta propeller domain]] | [[Category: beta propeller domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:23:07 2008'' |
Revision as of 21:23, 30 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Acylaminoacyl-peptidase, with EC number 3.4.19.1 | ||||||
| Related: | 1VE7
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1
Overview
Acylpeptide hydrolases (APH; also known as acylamino acid releasing enzyme) catalyze the removal of an N-acylated amino acid from blocked peptides. The crystal structure of an APH from the thermophilic archaeon Aeropyrum pernix K1 to 2.1 A resolution confirms it to be a member of the prolyl oligopeptidase family of serine proteases. The structure of apAPH is a symmetric homodimer with each subunit comprised of two domains. The N-terminal domain is a regular seven-bladed beta-propeller, while the C-terminal domain has a canonical alpha/beta hydrolase fold and includes the active site and a conserved Ser445-Asp524-His556 catalytic triad. The complex structure of apAPH with an organophosphorus substrate, p-nitrophenyl phosphate, has also been determined. The complex structure unambiguously maps out the substrate binding pocket and provides a basis for substrate recognition by apAPH. A conserved mechanism for protein degradation from archaea to mammals is suggested by the structural features of apAPH.
About this Structure
1VE6 is a Single protein structure of sequence from Aeropyrum pernix. Full crystallographic information is available from OCA.
Reference
Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1., Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z, Structure. 2004 Aug;12(8):1481-8. PMID:15296741
Page seeded by OCA on Mon Mar 31 00:23:07 2008
