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Yorodumi- PDB-4gch: STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4gch | ||||||
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Title | STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO 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: 1.9 Å | ||||||
Authors | Stoddard, B.L. / Ringe, D. / Petsko, G.A. | ||||||
Citation | Journal: Biochemistry / Year: 1990 Title: Structure and activity of two photoreversible cinnamates bound to chymotrypsin. Authors: Stoddard, B.L. / Bruhnke, J. / Porter, N. / Ringe, D. / Petsko, G.A. #1: Journal: Biochemistry / Year: 1990 Title: Photolysis and Deacylation of Inhibited Chymotrypsin Authors: Stoddard, B.L. / Bruhnke, J. / Koenig, P. / Porter, N. / Ringe, D. / Petsko, G.A. #2: Journal: Biochemistry / Year: 1990 Title: 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: Biochemistry / Year: 1990 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 | 4gch.cif.gz | 58.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4gch.ent.gz | 42.5 KB | Display | PDB format |
PDBx/mmJSON format | 4gch.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4gch_validation.pdf.gz | 404.1 KB | Display | wwPDB validaton report |
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Full document | 4gch_full_validation.pdf.gz | 425.8 KB | Display | |
Data in XML | 4gch_validation.xml.gz | 10.6 KB | Display | |
Data in CIF | 4gch_validation.cif.gz | 14.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gc/4gch ftp://data.pdbj.org/pub/pdb/validation_reports/gc/4gch | HTTPS FTP |
-Related structure data
-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: Chemical | ChemComp-DMC / |
#5: 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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Crystal grow | *PLUS pH: 5.6 / Method: other | ||||||||||||||||||||||||||||||
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 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. obs: 10856 / Rmerge(I) obs: 0.052 |
-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.9→45 Å /
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Refinement step | Cycle: LAST / Resolution: 1.9→45 Å
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Refine LS restraints |
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Refinement | *PLUS σ(I): 2 / Highest resolution: 1.9 Å / Lowest resolution: 45 Å / Num. reflection obs: 10856 / Rfactor obs: 0.209 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |