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1zap
From Proteopedia
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|PDB= 1zap |SIZE=350|CAPTION= <scene name='initialview01'>1zap</scene>, resolution 2.5Å | |PDB= 1zap |SIZE=350|CAPTION= <scene name='initialview01'>1zap</scene>, resolution 2.5Å | ||
|SITE= <scene name='pdbsite=ACT:Aspartic+Proteinases+Are+Characterized+By+Two+ASP+Residu+...'>ACT</scene> | |SITE= <scene name='pdbsite=ACT:Aspartic+Proteinases+Are+Characterized+By+Two+ASP+Residu+...'>ACT</scene> | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=A70:(2S)-2-[(3R)-3-BENZYL-4-N-(4-METHYLPIPERAZIN-1-YL-CARBONYL)2-KETOPIPERAZIN-1-YL]-HEXANOIC+ACID+AMIDE+OF+(2R,4S,5S)-5-AMINO-6-CYCLOHEXYL-4-HYDROXY-2-ISO-PROPYLHEXANOYL+N-(N-AMIDE)'>A70</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zap OCA], [http://www.ebi.ac.uk/pdbsum/1zap PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zap RCSB]</span> | ||
}} | }} | ||
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[[Category: Abad-Zapatero, C.]] | [[Category: Abad-Zapatero, C.]] | ||
[[Category: Muchmore, S W.]] | [[Category: Muchmore, S W.]] | ||
| - | [[Category: A70]] | ||
| - | [[Category: ZN]] | ||
[[Category: aspartic protease]] | [[Category: aspartic protease]] | ||
[[Category: candida albican]] | [[Category: candida albican]] | ||
[[Category: secreted]] | [[Category: secreted]] | ||
| - | ''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 01:33:14 2008'' |
Revision as of 22:33, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Candidapepsin, with EC number 3.4.23.24 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SECRETED ASPARTIC PROTEASE FROM C. ALBICANS
Overview
The three-dimensional structure of a secreted aspartic protease from Candida albicans complexed with a potent inhibitor reveals variations on the classical aspartic protease theme that dramatically alter the specificity of this class of enzymes. The structure presents: (1) an 8-residue insertion near the first disulfide (Cys 45-Cys 50, pepsin numbering) that results in a broad flap extending toward the active site; (2) a 7-residue deletion replacing helix hN2 (Ser 110-Tyr 114), which enlarges the S3 pocket; (3) a short polar connection between the two rigid body domains that alters their relative orientation and provides certain specificity; and (4) an ordered 11-residue addition at the carboxy terminus. The inhibitor binds in an extended conformation and presents a branched structure at the P3 position. The implications of these findings for the design of potent antifungal agents are discussed.
About this Structure
1ZAP is a Single protein structure of sequence from Candida albicans. Full crystallographic information is available from OCA.
Reference
Structure of a secreted aspartic protease from C. albicans complexed with a potent inhibitor: implications for the design of antifungal agents., Abad-Zapatero C, Goldman R, Muchmore SW, Hutchins C, Stewart K, Navaza J, Payne CD, Ray TL, Protein Sci. 1996 Apr;5(4):640-52. PMID:8845753
Page seeded by OCA on Mon Mar 31 01:33:14 2008
