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- PDB-1esb: DIRECT STRUCTURE OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN TH... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1esb | ||||||
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Title | DIRECT STRUCTURE OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASE | ||||||
![]() | PORCINE PANCREATIC ELASTASE | ||||||
![]() | HYDROLASE / SERINE PROTEINASE | ||||||
Function / homology | ![]() pancreatic elastase / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Ding, X. / Rasmussen, B. / Petsko, G.A. / Ringe, D. | ||||||
![]() | ![]() 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. #1: ![]() Title: Crystal Structure of the Covalent Complex Formed by a Peptidyl Alpha,Alpha-Difluoro-Beta-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. #2: ![]() Title: Structure of Native Procine Pancreatic Elastase at 1.65 Angstroms Resolution Authors: Meyer, E. / Cole, G. / Radhakrishnan, R. / Epp, O. #3: ![]() Title: Structures of Product and Inhibitor Complexes of Streptomyces Griseus Protease a at 1.8 Angstroms Resolution Authors: James, M.N.G. / Sielecki, A.R. / Brayer, G.D. / Delbaere, L.T.J. #4: ![]() Title: Formation of Stable Crystalline Enzyme-Substrate Intermediates at Sub-Zero Temperatures Authors: Fink, A.L. / Ahmed, A.I. #5: ![]() Title: Crystal Structure of Elastase-Substrate Complex at-55 Degc Authors: Alber, T. / Petsko, G.A. / Tsernoglou, D. | ||||||
History |
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Remark 700 | SHEET THE SHEETS PRESENTED AS *S1* AND *S2* ON SHEET RECORDS BELOW ARE ACTUALLY SIX-STRANDED BETA- ...SHEET THE SHEETS PRESENTED AS *S1* AND *S2* ON SHEET RECORDS BELOW ARE ACTUALLY SIX-STRANDED BETA-BARRELS. THIS IS REPRESENTED BY SEVEN-STRANDED SHEETS IN WHICH THE FIRST AND LAST STRAND OF EACH SHEET ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 62.5 KB | Display | ![]() |
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PDB format | ![]() | 45.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 392.8 KB | Display | ![]() |
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Full document | ![]() | 402.8 KB | Display | |
Data in XML | ![]() | 8.1 KB | Display | |
Data in CIF | ![]() | 11.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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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.) ![]() ![]() |
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#2: Chemical | ChemComp-BBL / |
#3: Chemical | ChemComp-CA / |
#4: Chemical | ChemComp-SO4 / |
#5: Water | ChemComp-HOH / |
Nonpolymer details | BBL IS COVALENTLY LINKED TO SER 203. THE P-NITROPHENYL GROUP ORIGINALLY PRESENT IN BBL MOLECULE IS ...BBL IS COVALENTLY |
Sequence details | THE RESIDUE NUMBERING SCHEME FOR THE PROTEIN IS SEQUENTIAL STARTING WITH VAL 16 AND ENDING WITH ASN ...THE RESIDUE NUMBERING SCHEME FOR THE PROTEIN IS SEQUENTIAL |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.42 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 2 ℃ / pH: 5 / Method: unknown / Details: Sawyer, L., (1978) J. Mol. Biol., 118, 137. | ||||||||||||||||||||
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: 2.3 Å / Lowest resolution: 11 Å / Num. all: 10437 / Num. obs: 10437 / % possible obs: 97 % |
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Processing
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Refinement | Resolution: 2.3→10 Å / Rfactor Rwork: 0.21 / Rfactor obs: 0.21 / σ(F): 1 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→10 Å
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Software | *PLUS Name: ![]() | ||||||||||||
Refinement | *PLUS Rfactor obs: 0.21 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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