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- PDB-5gch: CHEMISTRY OF CAGED ENZYMES /II$. PHOTOACTIVATION OF INHIBITED CHY... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5gch | ||||||
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Title | CHEMISTRY OF CAGED ENZYMES /II$. PHOTOACTIVATION OF INHIBITED CHYMOTRYPSIN | ||||||
![]() | (GAMMA-CHYMOTRYPSIN A) x 3 | ||||||
![]() | HYDROLASE (SERINE PROTEINASE) | ||||||
Function / homology | ![]() chymotrypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase activity / proteolysis / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Stoddard, B.L. / Ringe, D. / Petsko, G.A. | ||||||
![]() | ![]() Title: Photolysis and deacylation of inhibited chymotrypsin. Authors: Stoddard, B.L. / Bruhnke, J. / Koenigs, P. / Porter, N. / Ringe, D. / Petsko, G.A. #1: ![]() 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: ![]() 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: ![]() Title: Inhibition of Chymotrypsin by Peptidyl Trifluoromethy Ketones. Determinants of Slow-Binding Kinetics Authors: Brady, K. / Abeles, R.H. #4: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 56.9 KB | Display | ![]() |
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PDB format | ![]() | 41.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 383.7 KB | Display | ![]() |
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Full document | ![]() | 402 KB | Display | |
Data in XML | ![]() | 9.5 KB | Display | |
Data in CIF | ![]() | 13.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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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) ![]() ![]() |
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#2: Protein | Mass: 13934.556 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#3: Protein | Mass: 10074.495 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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 |
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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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