[English] 日本語
Yorodumi- PDB-1epm: A STRUCTURAL COMPARISON OF 21 INHIBITOR COMPLEXES OF THE ASPARTIC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1epm | ||||||
---|---|---|---|---|---|---|---|
Title | A STRUCTURAL COMPARISON OF 21 INHIBITOR COMPLEXES OF THE ASPARTIC PROTEINASE FROM ENDOTHIA PARASITICA | ||||||
Components |
| ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / ACID PROTEINASE / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Cryphonectria parasitica (chestnut blight fungus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.6 Å | ||||||
Authors | Crawford, M. / Cooper, J.B. / Strop, P. / Blundell, T.L. | ||||||
Citation | Journal: Protein Sci. / Year: 1994 Title: A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica. Authors: Bailey, D. / Cooper, J.B. #1: Journal: J.Mol.Biol. / Year: 1990 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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1epm.cif.gz | 76 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1epm.ent.gz | 57.6 KB | Display | PDB format |
PDBx/mmJSON format | 1epm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ep/1epm ftp://data.pdbj.org/pub/pdb/validation_reports/ep/1epm | HTTPS FTP |
---|
-Related structure data
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: CIS PROLINE - PRO E 23 / 2: CIS PROLINE - PRO E 133 |
-Components
#1: Protein | Mass: 33813.855 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Cryphonectria parasitica (chestnut blight fungus) References: UniProt: P11838, endothiapepsin | ||||||
---|---|---|---|---|---|---|---|
#2: Protein/peptide | Mass: 1056.192 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source | ||||||
#3: Chemical | #4: Water | ChemComp-HOH / | Nonpolymer details | RESIDUE I 5 IS A STANDARD THR. RESIDUE I 4 IS A STANDARD PHE. RESIDUE I 3 IS A STANDARD GLN. ...RESIDUE I 5 IS A STANDARD THR. RESIDUE I 4 IS A STANDARD PHE. RESIDUE I 3 IS A STANDARD GLN. RESIDUE I 2 IS A STANDARD ALA. 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: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38.54 % |
---|---|
Crystal grow | *PLUS Method: unknown |
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
-Processing
Software | Name: RESTRAIN / Classification: refinement | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.6→20 Å / Rfactor obs: 0.17 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→20 Å
| ||||||||||||
Software | *PLUS Name: RESTRAIN / Classification: refinement | ||||||||||||
Refinement | *PLUS Rfactor obs: 0.17 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |