+Open data
-Basic information
Entry | Database: PDB / ID: 1ewl | ||||||
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Title | CRYSTAL STRUCTURE OF CRUZAIN BOUND TO WRR-99 | ||||||
Components | CRUZAIN | ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / papain-like cysteine protease / drug design / covalent inhibitor / cruzipain / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | Function and homology information cruzipain / proteolysis involved in protein catabolic process / lysosome / cysteine-type endopeptidase activity / extracellular space Similarity search - Function | ||||||
Biological species | Trypanosoma cruzi (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Brinen, L.S. / Gillmor, S.A. / Fletterick, R.J. | ||||||
Citation | Journal: To be Published Title: Crystal Structure of Cruzain bound to WRR-99 Authors: Brinen, L.S. / Gillmor, S.A. / Fletterick, R.J. #1: Journal: Enzyme-ligand Interactions, Inhibition and Specificity Year: 1998 Title: Chapter 3: X-ray Structures of Complexes of Cruzain with Designed Covalent Inhibitors Authors: Gillmor, S.A. #2: Journal: Protein Sci. / Year: 1997 Title: Structural Determinants of Specificity in the Cysteine Protease Cruzain Authors: Gillmor, S.A. / Craik, C.S. / Fletterick, R.J. #3: Journal: J.Mol.Biol. / Year: 1995 Title: The Crystal Structure of Cruzain: a Therapeutic Target for Chagas' Disease Authors: McGrath, M.E. / Eakin, A.E. / Engel, J.C. / McKerrow, J.H. / Craik, C.S. / Fletterick, R.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ewl.cif.gz | 51.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ewl.ent.gz | 39.3 KB | Display | PDB format |
PDBx/mmJSON format | 1ewl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ewl_validation.pdf.gz | 757.3 KB | Display | wwPDB validaton report |
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Full document | 1ewl_full_validation.pdf.gz | 760.5 KB | Display | |
Data in XML | 1ewl_validation.xml.gz | 11 KB | Display | |
Data in CIF | 1ewl_validation.cif.gz | 14.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ew/1ewl ftp://data.pdbj.org/pub/pdb/validation_reports/ew/1ewl | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 22715.133 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma cruzi (eukaryote) / Plasmid: CHEY / Production host: Escherichia coli (E. coli) / Strain (production host): DH5ALPHA References: UniProt: P25779, Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases |
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#2: Chemical | ChemComp-R99 / |
#3: Water | ChemComp-HOH / |
Nonpolymer details | R99 IS AN E-64 ANALOG. R99 WAS N-(3-CARBOXYOXIRANE-2-CARBONYL)-D- HOMOPHENYLALANYL-AMINO-2- ...R99 IS AN E-64 ANALOG. R99 WAS N-(3-CARBOXYOXI |
Sequence details | THERE IS A STOP CODON AFTER RESIDUE 212. |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.81 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 6.25 Details: 0.9M NaCitrate, pH 6.25, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Feb 25, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→22 Å / Num. all: 11856 / Num. obs: 11856 / % possible obs: 96.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 2.2 % / Biso Wilson estimate: 11.7 Å2 / Rmerge(I) obs: 0.085 / Net I/σ(I): 8.1 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.169 / Num. unique all: 1185 / % possible all: 95.1 |
-Processing
Software |
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Refinement | Resolution: 2→22 Å / Rfactor Rfree error: 0.01 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: param19 and toph19 Details: used simulated annealing, positional, and isotropic bfactor refinement
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Displacement parameters | Biso mean: 16 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→22 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.13 Å / Rfactor Rfree error: 0.03 / Total num. of bins used: 6
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Xplor file |
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