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- PDB-1esa: 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: 1esa | ||||||
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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: Structure of Native Procine Pancreatic Elastase at 1.65 Angstroms Resolution Authors: Meyer, E. / Cole, G. / Radhakrishnan, R. / Epp, O. | ||||||
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 | ![]() | 60.9 KB | Display | ![]() |
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PDB format | ![]() | 44.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 380.4 KB | Display | ![]() |
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Full document | ![]() | 388.7 KB | Display | |
Data in XML | ![]() | 7.1 KB | Display | |
Data in CIF | ![]() | 10.8 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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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-CA / | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | 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: 2.16 Å3/Da / Density % sol: 42.97 % | ||||||||||||||||||||
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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: 1.65 Å / Lowest resolution: 23 Å / Num. all: 18435 / Num. obs: 16146 / % possible obs: 95 % |
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Processing
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Refinement | Resolution: 1.65→10 Å / Rfactor obs: 0.19 / σ(F): 1 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.65→10 Å
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Refinement | *PLUS Rfactor obs: 0.19 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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