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1zap

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[[Image:1zap.gif|left|200px]]<br /><applet load="1zap" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zap.gif|left|200px]]
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caption="1zap, resolution 2.5&Aring;" />
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'''SECRETED ASPARTIC PROTEASE FROM C. ALBICANS'''<br />
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{{Structure
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|PDB= 1zap |SIZE=350|CAPTION= <scene name='initialview01'>1zap</scene>, resolution 2.5&Aring;
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|SITE= <scene name='pdbsite=ACT:Aspartic+Proteinases+Are+Characterized+By+Two+ASP+Residu+...'>ACT</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <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>
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|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]
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|GENE=
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}}
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'''SECRETED ASPARTIC PROTEASE FROM C. ALBICANS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ZAP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=A70:'>A70</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=ACT:Aspartic+Proteinases+Are+Characterized+By+Two+ASP+Residu+...'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZAP OCA].
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1ZAP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZAP OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8845753 8845753]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8845753 8845753]
[[Category: Candida albicans]]
[[Category: Candida albicans]]
[[Category: Candidapepsin]]
[[Category: Candidapepsin]]
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[[Category: ZN]]
[[Category: ZN]]
[[Category: aspartic protease]]
[[Category: aspartic protease]]
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[[Category: candida albicans]]
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[[Category: candida albican]]
[[Category: secreted]]
[[Category: secreted]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:33:17 2008''

Revision as of 13:33, 20 March 2008


PDB ID 1zap

Drag the structure with the mouse to rotate
, resolution 2.5Å
Sites:
Ligands: and
Activity: Candidapepsin, with EC number 3.4.23.24
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

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