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Yorodumi- PDB-1gmh: REFINED CRYSTAL STRUCTURE OF "AGED" AND "NON-AGED" ORGANOPHOSPHOR... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1gmh | ||||||
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Title | REFINED CRYSTAL STRUCTURE OF "AGED" AND "NON-AGED" ORGANOPHOSPHORYL CONJUGATES OF GAMMA-CHYMOTRYPSIN | ||||||
Components | (GAMMA-CHYMOTRYPSIN ...) 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 | Harel, M. / Sussman, J.L. / Silman, I. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1991 Title: Refined crystal structures of "aged" and "non-aged" organophosphoryl conjugates of gamma-chymotrypsin. Authors: Harel, M. / Su, C.T. / Frolow, F. / Ashani, Y. / Silman, I. / Sussman, J.L. #1: Journal: Biochemistry / Year: 1991 Title: Gamma-Chymotrypsin is a Complex of Alpha-Chymotrypsin with its Own Autolysis Products Authors: Harel, M. / Su, C.-T. / Frolow, F. / Silman, I. / Sussman, J.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gmh.cif.gz | 53.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gmh.ent.gz | 37.5 KB | Display | PDB format |
PDBx/mmJSON format | 1gmh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1gmh_validation.pdf.gz | 410.6 KB | Display | wwPDB validaton report |
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Full document | 1gmh_full_validation.pdf.gz | 415.8 KB | Display | |
Data in XML | 1gmh_validation.xml.gz | 7.2 KB | Display | |
Data in CIF | 1gmh_validation.cif.gz | 10.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gm/1gmh ftp://data.pdbj.org/pub/pdb/validation_reports/gm/1gmh | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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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 |
-Non-polymers , 3 types, 105 molecules
#4: Chemical | #5: Chemical | ChemComp-ISP / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.37 % | |||||||||||||||
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Crystal grow | *PLUS pH: 5.5 / Method: unknown / Details: Cohen, G.H., (1981) J. Mol. Biol., 148, 449. | |||||||||||||||
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 / Num. all: 31167 / Num. obs: 11120 / Observed criterion σ(F): 3 / Rmerge(I) obs: 0.068 |
-Processing
Software | Name: PROLSQ / Version: 1GMH / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.1→6 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.1→6 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.187 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |