This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ve7
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ve7 |SIZE=350|CAPTION= <scene name='initialview01'>1ve7</scene>, resolution 2.7Å | |PDB= 1ve7 |SIZE=350|CAPTION= <scene name='initialview01'>1ve7</scene>, resolution 2.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=4NP:4-NITROPHENYL+PHOSPHATE'>4NP</scene> | + | |LIGAND= <scene name='pdbligand=4NP:4-NITROPHENYL+PHOSPHATE'>4NP</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=[[1ve6|1VE6]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ve7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ve7 OCA], [http://www.ebi.ac.uk/pdbsum/1ve7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ve7 RCSB]</span> | ||
}} | }} | ||
| Line 32: | Line 35: | ||
[[Category: Yang, H.]] | [[Category: Yang, H.]] | ||
[[Category: Zhao, X.]] | [[Category: Zhao, X.]] | ||
| - | [[Category: 4NP]] | ||
| - | [[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 00:23:09 2008'' |
Revision as of 21:23, 30 March 2008
| |||||||
| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Acylaminoacyl-peptidase, with EC number 3.4.19.1 | ||||||
| Related: | 1VE6
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate
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
1VE7 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 00:23:09 2008
