1n51
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1n51 |SIZE=350|CAPTION= <scene name='initialview01'>1n51</scene>, resolution 2.30Å | |PDB= 1n51 |SIZE=350|CAPTION= <scene name='initialview01'>1n51</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=ATN:N-[(2S,3R)-3-AMINO-2-HYDROXY-4-PHENYL-BUTANOYL]-L-PROLYL-L-PROLYL-L-ALANINAMIDE'>ATN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] </span> |
|GENE= PEPP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= PEPP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1az9|1AZ9]], [[1a16|1A16]], [[1jaw|1JAW]], [[1m35|1M35]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n51 OCA], [http://www.ebi.ac.uk/pdbsum/1n51 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n51 RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Maher, M J.]] | [[Category: Maher, M J.]] | ||
[[Category: Simmons, W H.]] | [[Category: Simmons, W H.]] | ||
| - | [[Category: ATN]] | ||
| - | [[Category: MN]] | ||
[[Category: aminopeptidase]] | [[Category: aminopeptidase]] | ||
[[Category: inhibitor complex]] | [[Category: inhibitor complex]] | ||
| Line 36: | Line 37: | ||
[[Category: proline specific]] | [[Category: proline specific]] | ||
| - | ''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 22:25:27 2008'' |
Revision as of 19:25, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | PEPP (Escherichia coli) | ||||||
| Activity: | Xaa-Pro aminopeptidase, with EC number 3.4.11.9 | ||||||
| Related: | 1AZ9, 1A16, 1JAW, 1M35
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Aminopeptidase P in complex with the inhibitor apstatin
Overview
Aminopeptidase P (APPro) is a metalloprotease whose active site includes a dinuclear manganese(II) cluster. The enzyme cleaves the N-terminal residue from a polypeptide when the second residue is proline. A complex of Escherichia coli APPro (EcAPPro) with an inhibitor, apstatin [N-(2S,3R)-3-amino-2-hydroxy-4-phenyl-butanoyl-L-prolyl-L-prolyl-L-alanina mide], has been crystallized. Apstatin binds to the active site of EcAPPro with its N-terminal amino group coordinated to one of the two Mn(II) atoms at the metal centre. The apstatin hydroxyl group replaces a hydroxide ion which bridges the two metal atoms in the native enzyme. The first proline residue of apstatin lies in a small hydrophobic cleft. The structure of the apstatin-EcAPPro complex has been refined at 2.3 A resolution with residuals R = 0.179 and R(free) = 0.204. The structure of the complex illustrates how apstatin inhibits APPro and suggests how substrates may bind to the enzyme, but the basis of the proline-specificity remains elusive.
About this Structure
1N51 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin., Graham SC, Maher MJ, Simmons WH, Freeman HC, Guss JM, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1770-9. Epub 2004, Sep 23. PMID:15388923
Page seeded by OCA on Sun Mar 30 22:25:27 2008
