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Yorodumi- PDB-2xtt: Bovine trypsin in complex with evolutionary enhanced Schistocerca... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2xtt | ||||||
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Title | Bovine trypsin in complex with evolutionary enhanced Schistocerca gregaria protease inhibitor 1 (SGPI-1-P02) | ||||||
Components |
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Keywords | HYDROLASE / CATALYTIC MECHANISM / INHIBITION / IN VITRO EVOLUTION | ||||||
Function / homology | Function and homology information trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase inhibitor activity / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | BOS TAURUS (cattle) SCHISTOCERCA GREGARIA (desert locust) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 0.93 Å | ||||||
Authors | Wahlgren, W.Y. / Pal, G. / Kardos, J. / Porrogi, P. / Szenthe, B. / Patthy, A. / Graf, L. / Katona, G. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2011 Title: The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease action. Authors: Wahlgren, W.Y. / Pal, G. / Kardos, J. / Porrogi, P. / Szenthe, B. / Patthy, A. / Graf, L. / Katona, G. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2xtt.cif.gz | 171 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2xtt.ent.gz | 137.2 KB | Display | PDB format |
PDBx/mmJSON format | 2xtt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2xtt_validation.pdf.gz | 439.2 KB | Display | wwPDB validaton report |
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Full document | 2xtt_full_validation.pdf.gz | 440.5 KB | Display | |
Data in XML | 2xtt_validation.xml.gz | 15.2 KB | Display | |
Data in CIF | 2xtt_validation.cif.gz | 23.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xt/2xtt ftp://data.pdbj.org/pub/pdb/validation_reports/xt/2xtt | HTTPS FTP |
-Related structure data
Related structure data | 1k1jS S: Starting model for refinement |
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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/peptide | Mass: 3932.404 Da / Num. of mol.: 1 / Fragment: RESIDUES 20-54 / Source method: obtained synthetically / Details: IN VITRO EVOLVED SEQUENCE WITH THE FOLLOWING / Source: (synth.) SCHISTOCERCA GREGARIA (desert locust) / References: UniProt: O46162 |
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#2: Protein | Mass: 23324.287 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Cell: ACINAR CELLS / Organ: PANCREAS / Tissue: GLANDULAR / References: UniProt: P00760, trypsin |
#3: Chemical | ChemComp-CA / |
#4: Chemical | ChemComp-ACT / |
#5: Water | ChemComp-HOH / |
Sequence details | IN VITRO EVOLVED SEQUENCE FOR CHAIN A. |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.89 Å3/Da / Density % sol: 34.9 % / Description: NONE |
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Crystal grow | pH: 4.6 Details: EQUAL AMOUNT OF PROTEIN SOLUTION (9.1 MG/ML PROTEIN COMPLEX IN 0.5 MM MES PH 6.0 BUFFER) AND PRECIPITANT SOLUTION (30% PEG 4000, 0.3 M AMMONIUM ACETATE, 0.1 M NA-ACETATE PH 4.6) WERE MIXED ...Details: EQUAL AMOUNT OF PROTEIN SOLUTION (9.1 MG/ML PROTEIN COMPLEX IN 0.5 MM MES PH 6.0 BUFFER) AND PRECIPITANT SOLUTION (30% PEG 4000, 0.3 M AMMONIUM ACETATE, 0.1 M NA-ACETATE PH 4.6) WERE MIXED AND EQUILIBRATED AGAINST 0.5 ML PRECIPITANT SOLUTION. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.9334 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Sep 30, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9334 Å / Relative weight: 1 |
Reflection | Resolution: 0.93→43.8 Å / Num. obs: 135272 / % possible obs: 91.3 % / Observed criterion σ(I): 2 / Redundancy: 3.4 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 17.9 |
Reflection shell | Resolution: 0.93→0.98 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 2.2 / % possible all: 54 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1K1J Resolution: 0.93→10 Å / Num. parameters: 20959 / Num. restraintsaints: 25983 / Cross valid method: FREE R-VALUE / σ(F): 0 StereochEM target val spec case: ASP-102, HIS-57, SER-195, ASP-194, GLY-193, SER-214 AND SCISSILE PEPTIDE BOND OF INHIBITOR Stereochemistry target values: ENGH AND HUBER Details: ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY 0.044. THE STRUCTURE WAS REFINED USING UNMERGED REFLECTIONS IN SHELX. THIS DATASET IS INCLUDED WITH THE MAIN STRUCTURE FACTOR FILE ...Details: ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY 0.044. THE STRUCTURE WAS REFINED USING UNMERGED REFLECTIONS IN SHELX. THIS DATASET IS INCLUDED WITH THE MAIN STRUCTURE FACTOR FILE R2XTTSF AS A SECOND DATASET.
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Refine analyze | Num. disordered residues: 21 / Occupancy sum hydrogen: 1820.58 / Occupancy sum non hydrogen: 2225.9 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 0.93→10 Å
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Refine LS restraints |
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