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Yorodumi- PDB-6gch: STRUCTURE OF CHYMOTRYPSIN-*TRIFLUOROMETHYL KETONE INHIBITOR COMPL... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6gch | ||||||
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Title | STRUCTURE OF CHYMOTRYPSIN-*TRIFLUOROMETHYL KETONE INHIBITOR COMPLEXES. COMPARISON OF SLOWLY AND RAPIDLY EQUILIBRATING INHIBITORS | ||||||
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: 2.1 Å | ||||||
Authors | Brady, K. / Wei, A. / Ringe, D. / Abeles, R.H. | ||||||
Citation | Journal: Biochemistry / Year: 1990 Title: Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors. Authors: Brady, K. / Wei, A.Z. / Ringe, D. / Abeles, R.H. #1: 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. #2: 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. #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 | 6gch.cif.gz | 60.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6gch.ent.gz | 44.3 KB | Display | PDB format |
PDBx/mmJSON format | 6gch.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6gch_validation.pdf.gz | 468.3 KB | Display | wwPDB validaton report |
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Full document | 6gch_full_validation.pdf.gz | 489.1 KB | Display | |
Data in XML | 6gch_validation.xml.gz | 10.9 KB | Display | |
Data in CIF | 6gch_validation.cif.gz | 15.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gc/6gch ftp://data.pdbj.org/pub/pdb/validation_reports/gc/6gch | HTTPS FTP |
-Related 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: 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-APF / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.73 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5.6 / Method: unknown | ||||||||||||||||||||||||||||||
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: 2.1 Å / % possible obs: 65 % / Observed criterion σ(I): 1 / Num. measured all: 9225 / Rmerge(I) obs: 0.065 |
-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.1→6 Å Details: 6GCH PHASES WERE CALCULATED FROM THE MODEL OF G.COHEN ET AL. 6GCH (PROTEIN DATA BANK ENTRY 2GCH) AND APPLIED TO STRUCTURE 6GCH FACTORS COLLATED FROM ALPHA-CHYMOTRYPSIN CRYSTALS WHICH HAD ...Details: 6GCH PHASES WERE CALCULATED FROM THE MODEL OF G.COHEN ET AL. 6GCH (PROTEIN DATA BANK ENTRY 2GCH) AND APPLIED TO STRUCTURE 6GCH FACTORS COLLATED FROM ALPHA-CHYMOTRYPSIN CRYSTALS WHICH HAD 6GCH BEEN SOAKED IN A SOLUTION CONTAINING THE INHIBITOR 6GCH N-ACETYL-L-PHENYLALANYL TRIFLUOROMETHYL KETONE. ALL 6GCH SECONDARY STRUCTURAL FEATURES AND SEQUENCE ARE IDENTICAL TO 6GCH PROTEIN DATA BANK ENTRY 2GCH. 6GCH
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Refinement step | Cycle: LAST / Resolution: 2.1→6 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 6 Å / Num. reflection obs: 9255 / Rfactor obs: 0.18 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 9.2 Å2 |