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Yorodumi- PDB-1gha: A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1gha | ||||||
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Title | A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE OF N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN | ||||||
Components |
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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: 2.2 Å | ||||||
Authors | Yennawar, H.P. / Yennawar, N.H. / Farber, G.K. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 1995 Title: A STRUCTURAL EXPLANATION FOR ENZYME MEMORY IN NONAQUEOUS SOLVENTS. Authors: Yennawar, H.P. / Yennawar, N.H. / Farber, G.K. #1: Journal: To be Published Title: X-Ray Crystal Structure of Gamma-Chymotrypsin in Hexane Authors: Yennawar, N.H. / Yennawar, H.P. / Farber, G.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gha.cif.gz | 58.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gha.ent.gz | 42 KB | Display | PDB format |
PDBx/mmJSON format | 1gha.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1gha_validation.pdf.gz | 402.1 KB | Display | wwPDB validaton report |
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Full document | 1gha_full_validation.pdf.gz | 407.4 KB | Display | |
Data in XML | 1gha_validation.xml.gz | 6.9 KB | Display | |
Data in CIF | 1gha_validation.cif.gz | 10.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gh/1gha ftp://data.pdbj.org/pub/pdb/validation_reports/gh/1gha | 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
-GAMMA-CHYMOTRYPSIN ... , 3 types, 3 molecules EFG
#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 |
-Protein/peptide , 1 types, 1 molecules P
#4: Protein/peptide | Mass: 434.486 Da / Num. of mol.: 1 / Source method: isolated from a natural source |
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-Non-polymers , 3 types, 175 molecules
#5: Chemical | ChemComp-SO4 / |
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#6: Chemical | ChemComp-IPA / |
#7: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.45 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5.6 / Method: batch method / Details: Yennawar, N. H., (1994) Biochemistry, 33, 7326. | ||||||||||||||||||||||||||||||
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: 2.2 Å / Num. obs: 15427 / Rmerge(I) obs: 0.097 |
-Processing
Software | Name: X-PLOR / Version: 1GHA / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor Rwork: 0.164 / Rfactor obs: 0.164 / Highest resolution: 2.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.2 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 5 Å / Rfactor obs: 0.164 / Rfactor Rwork: 0.164 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.63 |