1EAG

Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.195 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors.

Cutfield, S.M.Dodson, E.J.Anderson, B.F.Moody, P.C.E.Marshall, C.J.Sullivan, P.A.Cutfield, J.F.

(1995) Structure 3: 1261-1271

  • DOI: https://doi.org/10.1016/s0969-2126(01)00261-1
  • Primary Citation of Related Structures:  
    1EAG

  • PubMed Abstract: 

    Infections caused by Candida albicans, a common fungal pathogen of humans, are increasing in incidence, necessitating development of new therapeutic drugs. Secreted aspartic proteinase (SAP) activity is considered an important virulence factor in these infections and might offer a suitable target for drug design. Amongst the various SAP isozymes, the SAP2 gene product is the major form expressed in a number of C. albicans strains.


  • Organizational Affiliation

    Biochemistry Department, University of Otago, Dunedin, New Zealand.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ASPARTIC PROTEINASE (SAP2 GENE PRODUCT)342Candida albicansMutation(s): 0 
EC: 3.4.23.24
UniProt
Find proteins for P0CS83 (Candida albicans)
Explore P0CS83 
Go to UniProtKB:  P0CS83
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0CS83
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
A70
Query on A70

Download Ideal Coordinates CCD File 
B [auth A]N-ethyl-N-[(4-methylpiperazin-1-yl)carbonyl]-D-phenylalanyl-N-[(1S,2S,4R)-4-(butylcarbamoyl)-1-(cyclohexylmethyl)-2-hyd roxy-5-methylhexyl]-L-norleucinamide
C42 H70 N6 O5
NGCGSAFHWCZMPV-AKHKZFQHSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.195 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 76.2α = 90
b = 76.2β = 90
c = 126.1γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
PROLSQrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-12-23
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Atomic model, Database references, Derived calculations, Non-polymer description, Structure summary, Version format compliance
  • Version 1.3: 2012-01-18
    Changes: Non-polymer description