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- PDB-1epo: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH CP-8... -

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Basic information

Entry
Database: PDB / ID: 1epo
TitleENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH CP-81,282 (MOR PHE NLE CHF NME)
ComponentsENDOTHIAPEPSIN
KeywordsHYDROLASE/HYDROLASE INHIBITOR / ACID PROTEINASE / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homology
Function and homology information


endothiapepsin / aspartic-type endopeptidase activity / proteolysis
Similarity search - Function
Aspergillopepsin-like catalytic domain / Eukaryotic aspartyl protease / Aspartic peptidase A1 family / Peptidase family A1 domain / Peptidase family A1 domain profile. / Cathepsin D, subunit A; domain 1 / Acid Proteases / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily ...Aspergillopepsin-like catalytic domain / Eukaryotic aspartyl protease / Aspartic peptidase A1 family / Peptidase family A1 domain / Peptidase family A1 domain profile. / Cathepsin D, subunit A; domain 1 / Acid Proteases / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
CP-81,282, MOR-PHE-NLE-CHF-NME / Chem-2Z3 / Endothiapepsin
Similarity search - Component
Biological speciesCryphonectria parasitica (chestnut blight fungus)
MethodX-RAY DIFFRACTION / Resolution: 2 Å
AuthorsVeerapandian, B. / Cooper, J.B. / Blundell, T.L.
Citation
Journal: Protein Sci. / Year: 1992
Title: Direct observation by X-ray analysis of the tetrahedral intermediate of aspartic proteinases.
Authors: Veerapandian, B. / Cooper, J.B. / Sali, A. / Blundell, T.L. / Rosati, R.L. / Dominy, B.W. / Damon, D.B. / Hoover, D.J.
#1: Journal: To be Published
Title: A Structural Comparison of 21 Inhibitor Complexes of the Aspartic Proteinase from Endothia Parasitica
Authors: Bailey, D. / Cooper, J.B.
#2: 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
DepositionJul 27, 1994Processing site: BNL
Revision 1.0Dec 20, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 10, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Atomic model / Database references ...Atomic model / Database references / Derived calculations / Non-polymer description / Structure summary / Version format compliance
Revision 1.3Dec 12, 2012Group: Other
Revision 1.4Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
E: ENDOTHIAPEPSIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,4682
Polymers33,8141
Non-polymers6541
Water5,513306
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)53.700, 73.900, 45.800
Angle α, β, γ (deg.)90.00, 110.00, 90.00
Int Tables number4
Space group name H-MP1211
Atom site foot note1: CIS PROLINE - PRO E 23
2: ALA E 24 - GLN E 25 OMEGA = 147.33 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
3: SER E 81 - GLY E 82 OMEGA = 149.87 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
4: CIS PROLINE - PRO E 133
5: VAL E 150 - PHE E 151 OMEGA = 145.80 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
6: GLY E 245 - TYR E 246 OMEGA = 141.52 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
7: PHE E 275 - GLY E 276 OMEGA = 135.99 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION

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Components

#1: Protein ENDOTHIAPEPSIN /


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: Chemical ChemComp-2Z3 / N-(morpholin-4-ylcarbonyl)-L-phenylalanyl-N-[(1R)-1-(cyclohexylmethyl)-3,3-difluoro-2,2-dihydroxy-4-(methylamino)-4-oxobutyl]-L-norleucinamide / CP-81,282


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 653.758 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C32H49F2N5O7 / References: CP-81,282, MOR-PHE-NLE-CHF-NME
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 306 / Source method: isolated from a natural source / Formula: H2O
Nonpolymer detailsTHE INHIBITOR HAS A K(I) OF 11 NM FOR ENDOTHIAPEPSIN.
Sequence detailsRESIDUES 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 RELATIVE TO PORCINE PEPSIN.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.48 Å3/Da / Density % sol: 50.36 %
Crystal grow
*PLUS
pH: 6.3 / Method: unknown / Details: pH is adjusted to 6.3 with dilute sodium hydroxide
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
12.2 Mammonium sulfate11
30.1 Msodium dihydrogen phosphate11
40.25-0.1 %(w/v)acetone11
2acetate11or phosphate

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
Reflection
*PLUS
Highest resolution: 2 Å / Num. obs: 16999 / % possible obs: 76 % / Num. measured all: 42676 / Rmerge(I) obs: 0.074

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Processing

SoftwareName: RESTRAIN / Classification: refinement
RefinementResolution: 2→20 Å
Details: THE QUANTITY GIVEN IN THE TEMPERATURE FACTOR FIELD OF THE *ATOM* AND *HETATM* RECORDS BELOW IS U**2, WHICH IS THE MEAN-SQUARE AMPLITUDE OF ATOMIC VIBRATION. THE TEMPERATURE FACTOR, B, CAN BE ...Details: THE QUANTITY GIVEN IN THE TEMPERATURE FACTOR FIELD OF THE *ATOM* AND *HETATM* RECORDS BELOW IS U**2, WHICH IS THE MEAN-SQUARE AMPLITUDE OF ATOMIC VIBRATION. THE TEMPERATURE FACTOR, B, CAN BE DERIVED BY THE FOLLOWING RELATION: B = 8 * (PI)**2 * U**2.
RfactorNum. reflection
obs0.18 16999
Refinement stepCycle: LAST / Resolution: 2→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2389 0 46 306 2741
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONp_bond_d0.021
X-RAY DIFFRACTIONp_angle_d0.023
X-RAY DIFFRACTIONp_planar_d0.005
Software
*PLUS
Name: RESTRAIN / Classification: refinement
Refinement
*PLUS
σ(F): 2 / Rfactor obs: 0.18
Solvent computation
*PLUS
Displacement parameters
*PLUS

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