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- PDB-1epl: A STRUCTURAL COMPARISON OF 21 INHIBITOR COMPLEXES OF THE ASPARTIC... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1epl | ||||||
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Title | A STRUCTURAL COMPARISON OF 21 INHIBITOR COMPLEXES OF THE ASPARTIC PROTEINASE FROM ENDOTHIA PARASITICA | ||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / ACID PROTEINASE / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Al-Karadaghi, S. / Cooper, J.B. / Strop, P. / Blundell, T.L. | ||||||
![]() | ![]() Title: A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica. Authors: Bailey, D. / Cooper, J.B. #1: ![]() Title: The 3D Structure at 2 Angstroms Resolution of Endothiapepsin Authors: Blundell, T.L. / Jenkins, J. / Sewell, B.T. / Pearl, L.H. / Cooper, J.B. / Tickle, I.J. / Veerapandian, B. / Wood, S.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 74.7 KB | Display | ![]() |
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PDB format | ![]() | 57.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 376.4 KB | Display | ![]() |
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Full document | ![]() | 386.5 KB | Display | |
Data in XML | ![]() | 9.4 KB | Display | |
Data in CIF | ![]() | 15.3 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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Atom site foot note | 1: CIS PROLINE - PRO E 23 / 2: CIS PROLINE - PRO E 133 3: THR E 318 - THR E 319 OMEGA = 149.01 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
#1: Protein | Mass: 33813.855 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: P11838, endothiapepsin |
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#2: Protein/peptide | Mass: 818.980 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source |
#3: Water | ChemComp-HOH / |
Nonpolymer details | RESIDUE I 4 IS A STANDARD PRO. RESIDUE I 3 IS A STANDARD LEU. RESIDUE I 2 IS A STANDARD GLU. ...RESIDUE I 4 IS A STANDARD PRO. RESIDUE I 3 IS A STANDARD LEU. RESIDUE I 2 IS A STANDARD GLU. RESIDUE I 1 (PSA) IS A PHENYLSTAT |
Sequence details | RESIDUES 63A, 80A, 134A, 184A, 203A, 204A, 238A, 282A, 282B, AND 319A IN CHAIN E ARE INSERTIONS ...RESIDUES 63A, 80A, 134A, 184A, 203A, 204A, 238A, 282A, 282B, AND 319A IN CHAIN E ARE INSERTIONS |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.25 % |
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Crystal grow | *PLUS Method: unknown |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
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Processing
Software | Name: RESTRAIN / Classification: refinement | ||||||||||||
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Refinement | Resolution: 2→8 Å /
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Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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