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Yorodumi- PDB-5gch: CHEMISTRY OF CAGED ENZYMES /II$. PHOTOACTIVATION OF INHIBITED CHY... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5gch | ||||||
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Title | CHEMISTRY OF CAGED ENZYMES /II$. PHOTOACTIVATION OF INHIBITED CHYMOTRYPSIN | ||||||
Components | (GAMMA-CHYMOTRYPSIN A) x 3 | ||||||
Keywords | HYDROLASE (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: 2.7 Å | ||||||
Authors | Stoddard, B.L. / Ringe, D. / Petsko, G.A. | ||||||
Citation | Journal: Biochemistry / Year: 1990 Title: Photolysis and deacylation of inhibited chymotrypsin. Authors: Stoddard, B.L. / Bruhnke, J. / Koenigs, P. / Porter, N. / Ringe, D. / Petsko, G.A. #1: Journal: To be Published Title: Chemistry of Caged Enzymes. Binding of Photoreversible Cinnamates to Chymotrypsin Authors: Stoddard, B.L. / Bruhnke, J. / Porter, N. / Ringe, D. / Petsko, G.A. #2: Journal: To be Published Title: The Structure of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison of Slowly and Rapidly Equilibrating Inhibitors Authors: Brady, K. / Wei, A. / Ringe, D. / Abeles, R.H. #3: Journal: To be Published Title: Inhibition of Chymotrypsin by Peptidyl Trifluoromethy Ketones. Determinants of Slow-Binding Kinetics Authors: Brady, K. / Abeles, R.H. #4: Journal: Biochemistry / Year: 1989 Title: Ph Dependence of the Inhibition of Chymotrypsin by a Peptidyl Trifluoromethyl Ketone Authors: Liang, K.Brady.T.-C. / Abeles, R.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5gch.cif.gz | 53.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5gch.ent.gz | 42.4 KB | Display | PDB format |
PDBx/mmJSON format | 5gch.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gc/5gch ftp://data.pdbj.org/pub/pdb/validation_reports/gc/5gch | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein/peptide | Mass: 1253.511 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00766, chymotrypsin |
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#2: Protein | Mass: 13934.556 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00766, chymotrypsin |
#3: Protein | Mass: 10074.495 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00766, chymotrypsin |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.5 % |
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.7→50 Å /
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Refinement step | Cycle: LAST / Resolution: 2.7→50 Å
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Refine LS restraints |
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