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Yorodumi- PDB-1elg: NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDR... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1elg | ||||||
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Title | NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH | ||||||
Components | PORCINE PANCREATIC ELASTASE | ||||||
Keywords | COMPLEX (HYDROLASE/INHIBITOR) / COMPLEX (HYDROLASE-INHIBITOR) / COMPLEX (HYDROLASE-INHIBITOR) complex | ||||||
Function / homology | Function and homology information pancreatic elastase / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | Sus scrofa (pig) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.65 Å | ||||||
Authors | Ding, X. / Rasmussen, B. / Demuth, H.-U. / Ringe, D. / Steinmetz, A.C.U. | ||||||
Citation | Journal: Biochemistry / Year: 1995 Title: Nature of the inactivation of elastase by N-peptidyl-O-aroyl hydroxylamine as a function of pH. Authors: Ding, X. / Rasmussen, B.F. / Demuth, H.U. / Ringe, D. / Steinmetz, A.C. #1: Journal: Biochemistry / Year: 1994 Title: Direct Structural Observation of an Acyl-Enzyme Intermediate in the Hydrolysis of an Ester Substrate by Elastase Authors: Ding, X. / Rasmussen, B.F. / Petsko, G.A. / Ringe, D. #2: Journal: J.Enzyme Inhib. / Year: 1991 Title: Inhibition of Proteases with Enkephalin-Analogue Inhibitors Authors: Demuth, H.-U. / Silberring, J. / Nyberg, F. #3: Journal: J.Am.Chem.Soc. / Year: 1991 Title: Competing Redox and Inactivation Processes in the Inhibition of Cysteine Proteinases by Peptidyl O-Acylhydroxamates. 13C and 15N NMR Evidence for a Novel Sulfenamide Enzyme Adduct Authors: Robinson, V.J. / Coles, P.J. / Smith, R.A. / Krantz, A. #4: Journal: J.Org.Chem. / Year: 1989 Title: N-O Bond Fission as the Rate-Determining Step in the Aqueous Conversion of N-Peptiyl-O-(P-Nitrobenzoyl)Hydroxylamines to P-Nitrobenzoic Acid and Peptidylhydroxamic Acids Authors: Demuth, H.-U. / Fischer, G. / Barth, A. / Schowen, R.L. #5: Journal: J.Am.Chem.Soc. / Year: 1989 Title: Crystal Structure of the Covalent Complex Formed by a Peptidyl Difluoro Keto Amide with Porcine Pancreatic Elastase at 1.78 Angstroms Resolution Authors: Takahashi, L.H. / Radhakrishnan, R. / Rosenfield Junior, R.E. / Meyer Junior, E.F. / Trainor, D.A. | ||||||
History |
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Remark 700 | SHEET THE TWO SEVEN STRANDED SHEETS IN THIS STRUCTURE ARE REALLY SIX STRANDED BETA BARRELS. THIS IS ...SHEET THE TWO SEVEN STRANDED SHEETS IN THIS STRUCTURE ARE REALLY SIX STRANDED BETA BARRELS. THIS IS DENOTED BY THE FIRST STRAND RECURRING AS THE LAST STRAND. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1elg.cif.gz | 59.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1elg.ent.gz | 46.8 KB | Display | PDB format |
PDBx/mmJSON format | 1elg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/el/1elg ftp://data.pdbj.org/pub/pdb/validation_reports/el/1elg | HTTPS FTP |
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-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 | Mass: 25928.031 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / References: UniProt: P00772, pancreatic elastase |
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#2: Chemical | ChemComp-CA / |
#3: Chemical | ChemComp-BAA / ( |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.75 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
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 | Resolution: 1.65→10 Å / Num. obs: 23730 / % possible obs: 85 % / Observed criterion σ(I): 2 |
Reflection | *PLUS Lowest resolution: 44 Å / Num. obs: 27890 / % possible obs: 100 % / Observed criterion σ(I): 0 |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.17 / Rfactor obs: 0.17 / Highest resolution: 1.65 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.65 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 10 Å / Num. reflection all: 23730 / σ(I): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |