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Yorodumi- PDB-1eag: Secreted aspartic proteinase (SAP2) from Candida albicans complex... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1eag | ||||||
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Title | Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450 | ||||||
Components | ASPARTIC PROTEINASE (SAP2 GENE PRODUCT) | ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / SAP2 / CANDIDA ALBICANS / HYDROLASE-HYDROLASE INHIBITOR COMPLEX / ASPARTIC PROTEASE | ||||||
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: 2.1 Å | ||||||
Authors | Cutfield, J.F. / Cutfield, S.M. | ||||||
Citation | 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.E. / Marshall, C.J. / Sullivan, P.A. / Cutfield, J.F. #1: Journal: J.Mol.Biol. / Year: 1993 Title: Crystallization of Inhibited Aspartic Proteinase from Candida Albicans Authors: Cutfield, S. / Marshall, C. / Moody, P. / Sullivan, P. / Cutfield, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1eag.cif.gz | 75.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1eag.ent.gz | 60.1 KB | Display | PDB format |
PDBx/mmJSON format | 1eag.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1eag_validation.pdf.gz | 460 KB | Display | wwPDB validaton report |
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Full document | 1eag_full_validation.pdf.gz | 472.2 KB | Display | |
Data in XML | 1eag_validation.xml.gz | 9.8 KB | Display | |
Data in CIF | 1eag_validation.cif.gz | 14.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ea/1eag ftp://data.pdbj.org/pub/pdb/validation_reports/ea/1eag | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 36357.723 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Candida albicans (yeast) References: UniProt: P28871, UniProt: P0CS83*PLUS, candidapepsin |
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#2: Chemical | ChemComp-A70 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.52 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 6.2 / Method: vapor diffusion, hanging drop / Details: Cutfield, S., (1993) J.Mol.Biol., 234, 1266. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 24302 / % possible obs: 98 % / Redundancy: 7.5 % / Rmerge(I) obs: 0.072 |
Reflection | *PLUS Highest resolution: 2.05 Å |
-Processing
Software |
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Refinement | Resolution: 2.1→8 Å / σ(F): 0 Details: LOOP RESIDUES A 284, A 285, AND A 286 HAVE WEAK, DISORDERED DENSITY AND THEIR COORDINATES HAVE BEEN OMITTED.
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Displacement parameters | Biso mean: 32.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→8 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.195 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |