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Yorodumi- PDB-1chg: CHYMOTRYPSINOGEN,2.5 ANGSTROMS CRYSTAL STRUCTURE, COMPARISON WITH... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1chg | |||||||||
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Title | CHYMOTRYPSINOGEN,2.5 ANGSTROMS CRYSTAL STRUCTURE, COMPARISON WITH ALPHA-CHYMOTRYPSIN,AND IMPLICATIONS FOR ZYMOGEN ACTIVATION | |||||||||
Components | CHYMOTRYPSINOGEN A | |||||||||
Keywords | HYDROLASE ZYMOGEN (SERINE PROTEINASE) | |||||||||
Function / homology | Function and homology information chymotrypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase activity / proteolysis / extracellular region Similarity search - Function | |||||||||
Biological species | Bos taurus (cattle) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | |||||||||
Authors | Freer, S.T. / Kraut, J. / Robertus, J.D. / Wright, H.T. / Xuong, N.H. | |||||||||
Citation | Journal: Biochemistry / Year: 1970 Title: Chymotrypsinogen: 2.5-angstrom crystal structure, comparison with alpha-chymotrypsin, and implications for zymogen activation. Authors: Freer, S.T. / Kraut, J. / Robertus, J.D. / Wright, H.T. / Xuong, N.H. #1: Journal: The Enzymes,Third Edition / Year: 1971 Title: Chymotrypsinogen,X-Ray Structure Authors: Kraut, J. #2: Journal: J.Mol.Biol. / Year: 1973 Title: Comparison of the Crystal Structures of Chymotrypsinogen-A and Alpha-Chymotrypsin Authors: Wright, H.T. #3: Journal: J.Mol.Biol. / Year: 1973 Title: Activation of Chymotrypsinogen-A,an Hypothesis Based Upon Comparison of the Crystal Structures of Chymotrypsinogen-A and Alpha-Chymotrypsin Authors: Wright, H.T. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1chg.cif.gz | 57.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1chg.ent.gz | 35.1 KB | Display | PDB format |
PDBx/mmJSON format | 1chg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1chg_validation.pdf.gz | 372.4 KB | Display | wwPDB validaton report |
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Full document | 1chg_full_validation.pdf.gz | 476.4 KB | Display | |
Data in XML | 1chg_validation.xml.gz | 20.1 KB | Display | |
Data in CIF | 1chg_validation.cif.gz | 25.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ch/1chg ftp://data.pdbj.org/pub/pdb/validation_reports/ch/1chg | 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: 25686.037 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / References: UniProt: P00766 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.65 % | |||||||||||||||
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Crystal grow | *PLUS pH: 6.3 / Method: microdialysis | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Refinement | Rfactor Rwork: 0.43 / Highest resolution: 2.5 Å | ||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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