+Open data
-Basic information
Entry | Database: PDB / ID: 1zap | ||||||
---|---|---|---|---|---|---|---|
Title | SECRETED ASPARTIC PROTEASE FROM C. ALBICANS | ||||||
Components | SECRETED ASPARTIC PROTEINASE | ||||||
Keywords | ASPARTIC PROTEASE / SECRETED / CANDIDA ALBICANS | ||||||
Function / homology | Function and homology information : / protein catabolic process => GO:0030163 / candidapepsin / : / signal peptide processing / fungal-type cell wall organization / adhesion of symbiont to host / fungal-type cell wall / protein metabolic process / : ...: / protein catabolic process => GO:0030163 / candidapepsin / : / signal peptide processing / fungal-type cell wall organization / adhesion of symbiont to host / fungal-type cell wall / protein metabolic process / : / protein catabolic process / extracellular vesicle / aspartic-type endopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Candida albicans (yeast) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Abad-Zapatero, C. / Muchmore, S.W. | ||||||
Citation | Journal: Protein Sci. / Year: 1996 Title: Structure of a secreted aspartic protease from C. albicans complexed with a potent inhibitor: implications for the design of antifungal agents. Authors: Abad-Zapatero, C. / Goldman, R. / Muchmore, S.W. / Hutchins, C. / Stewart, K. / Navaza, J. / Payne, C.D. / Ray, T.L. #1: Journal: Structure / Year: 1995 Title: The Crystal Structure of a Major Secreted Aspartic Proteinase from Candida Albicans in Complexes with Two Inhibitors Authors: Cutfield, S.M. / Dodson, E.J. / Anderson, B.F. / Moody, P.C. / Marshall, C.J. / Sullivan, P.A. / Cutfield, J.F. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1zap.cif.gz | 96.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1zap.ent.gz | 78.8 KB | Display | PDB format |
PDBx/mmJSON format | 1zap.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/za/1zap ftp://data.pdbj.org/pub/pdb/validation_reports/za/1zap | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 36321.602 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: CLOSEST ATTC HOMOLOG IS SAP2 ISOLATED FROM C. ALBICANS Source: (natural) Candida albicans (yeast) / Variant: PATHOGENIC CLINICAL ISOLATE FROM SKIN / Strain: VAL-1 / Tissue: SKIN References: UniProt: P28871, UniProt: P0CS83*PLUS, candidapepsin |
---|---|
#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-A70 / |
#4: Water | ChemComp-HOH / |
Compound details | THIS ENZYME IS A VERY CLOSE HOMOLOGUE OF THE SECRETED ASPARTIC PROTEASE FROM C. ALBICANS (ATCC ...THIS ENZYME IS A VERY CLOSE HOMOLOGUE OF THE SECRETED ASPARTIC PROTEASE FROM C. ALBICANS (ATCC 10261) REFERRED TO AS SAP2. THE DEPOSITORS |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 41.96 % | ||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 4.5 / Method: unknown | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction source | Wavelength: 1.5418 |
---|---|
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Jun 1, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→8 Å / Num. obs: 10193 / % possible obs: 89 % / Observed criterion σ(I): 3.5 / Redundancy: 3 % / Rmerge(I) obs: 0.099 |
Reflection | *PLUS Num. measured all: 30743 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.5→8 Å / σ(F): 0 /
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|