D00441
type: Enzyme
rlcp: p966
cath: Cathepsin D, subunit A; domain 1
ec: https://purl.uniprot.org/enzyme/3.4.23.22
csa: 1eed
uniprot: P11838
kegg enzyme: endothiapepsin
kegg substrate: Protein
kegg substrate: Peptide
kegg substrate: H2O
kegg product: Protein
kegg product: Peptide
kegg intermediate: Amino-diol-tetrahedral intermediate
pdb: 1e5oE01
pdb: 1e80E01
pdb: 1e81E01
pdb: 1e82E01
pdb: 1eedP01
pdb: 1entE01
pdb: 1eplE01
pdb: 1epmE01
pdb: 1epnE01
pdb: 1epoE01
pdb: 1eppE01
pdb: 1epqE01
pdb: 1eprE01
pdb: 1er8E01
pdb: 1gktA01
pdb: 1gvtA01
pdb: 1gvuA01
pdb: 1gvvA01
pdb: 1gvwA01
pdb: 1gvxA01
pdb: 1od1A01
pdb: 1oewA01
pdb: 1oexA01
pdb: 2er0E01
pdb: 2er6E01
pdb: 2er7E01
pdb: 2er9E01
pdb: 3er3E01
pdb: 3er5E01
pdb: 4apeA01
pdb: 4er1E01
pdb: 4er2E01
pdb: 4er4E01
pdb: 5er1E01
pdb: 5er2E01
pdb: 1e5oE02
pdb: 1e80E02
pdb: 1e81E02
pdb: 1e82E02
pdb: 1eedP02
pdb: 1entE02
pdb: 1eplE02
pdb: 1epmE02
pdb: 1epnE02
pdb: 1epoE02
pdb: 1eppE02
pdb: 1epqE02
pdb: 1eprE02
pdb: 1er8E02
pdb: 1gktA02
pdb: 1gvtA02
pdb: 1gvuA02
pdb: 1gvvA02
pdb: 1gvwA02
pdb: 1gvxA02
pdb: 1od1A02
pdb: 1oewA02
pdb: 1oexA02
pdb: 2er0E02
pdb: 2er6E02
pdb: 2er7E02
pdb: 2er9E02
pdb: 3er3E02
pdb: 3er5E02
pdb: 4apeA02
pdb: 4er1E02
pdb: 4er2E02

Cathepsin D, subunit A; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.40.70.10
catalytic domain: index.html

Protein
type: KeggSubstrate
references: KEGG:C00017
compound type: peptide/protein
type: KeggProduct

Peptide
type: KeggSubstrate
references: KEGG:C00012
compound type: peptide/protein
type: KeggProduct

H2O
type: KeggSubstrate
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Amino-diol-tetrahedral intermediate
type: KeggIntermediate
references: KEGG:I00136

1e5oE01
type: Pdb
references: 1e5o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5o
catalytic residue: ASP 32

1e80E01
type: Pdb
references: 1e80
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e80
catalytic residue: ASP 32

1e81E01
type: Pdb
references: 1e81
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e81
catalytic residue: ASP 32

1e82E01
type: Pdb
references: 1e82
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e82
catalytic residue: ASP 32

1eedP01
type: Pdb
references: 1eed
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eed
catalytic residue: ASP 32

1entE01
type: Pdb
references: 1ent
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ent
catalytic residue: ASP 32

1eplE01
type: Pdb
references: 1epl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epl
catalytic residue: ASP 32

1epmE01
type: Pdb
references: 1epm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epm
catalytic residue: ASP 32

1epnE01
type: Pdb
references: 1epn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epn
catalytic residue: ASP 32

1epoE01
type: Pdb
references: 1epo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epo
catalytic residue: ASP 32

1eppE01
type: Pdb
references: 1epp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epp
catalytic residue: ASP 32

1epqE01
type: Pdb
references: 1epq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epq
catalytic residue: ASP 32

1eprE01
type: Pdb
references: 1epr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epr
catalytic residue: ASP 32

1er8E01
type: Pdb
references: 1er8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1er8
catalytic residue: ASP 32

1gktA01
type: Pdb
references: 1gkt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gkt
catalytic residue: ASP 35

1gvtA01
type: Pdb
references: 1gvt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvt
catalytic residue: ASP 35

1gvuA01
type: Pdb
references: 1gvu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvu
catalytic residue: ASP 35

1gvvA01
type: Pdb
references: 1gvv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvv
catalytic residue: ASP 35

1gvwA01
type: Pdb
references: 1gvw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvw
catalytic residue: ASP 35

1gvxA01
type: Pdb
references: 1gvx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvx
catalytic residue: ASP 35

1od1A01
type: Pdb
references: 1od1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1od1
catalytic residue: ASP 35

1oewA01
type: Pdb
references: 1oew
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oew
catalytic residue: ASP 35

1oexA01
type: Pdb
references: 1oex
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oex
catalytic residue: ASP 35

2er0E01
type: Pdb
references: 2er0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er0
catalytic residue: ASP 32

2er6E01
type: Pdb
references: 2er6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er6
catalytic residue: ASP 32

2er7E01
type: Pdb
references: 2er7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er7
catalytic residue: ASP 32

2er9E01
type: Pdb
references: 2er9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er9
catalytic residue: ASP 32

3er3E01
type: Pdb
references: 3er3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3er3
catalytic residue: ASP 32

3er5E01
type: Pdb
references: 3er5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3er5
catalytic residue: ASP 32

4apeA01
type: Pdb
references: 4ape
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4ape
catalytic residue: ASP 32

4er1E01
type: Pdb
references: 4er1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4er1
catalytic residue: ASP 32

4er2E01
type: Pdb
references: 4er2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4er2
catalytic residue: ASP 32

4er4E01
type: Pdb
references: 4er4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4er4
catalytic residue: ASP 32

5er1E01
type: Pdb
references: 5er1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5er1
catalytic residue: ASP 32

5er2E01
type: Pdb
references: 5er2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5er2
catalytic residue: ASP 32

1e5oE02
type: Pdb
references: 1e5o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5o
catalytic residue: ASP 215

1e80E02
type: Pdb
references: 1e80
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e80
catalytic residue: ASP 215

1e81E02
type: Pdb
references: 1e81
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e81
catalytic residue: ASP 215

1e82E02
type: Pdb
references: 1e82
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e82
catalytic residue: ASP 215

1eedP02
type: Pdb
references: 1eed
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eed
catalytic residue: ASP 215

1entE02
type: Pdb
references: 1ent
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ent
catalytic residue: ASP 215

1eplE02
type: Pdb
references: 1epl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epl
catalytic residue: ASP 215

1epmE02
type: Pdb
references: 1epm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epm
catalytic residue: ASP 215

1epnE02
type: Pdb
references: 1epn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epn
catalytic residue: ASP 215

1epoE02
type: Pdb
references: 1epo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epo
catalytic residue: ASP 215

1eppE02
type: Pdb
references: 1epp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epp
catalytic residue: ASP 215

1epqE02
type: Pdb
references: 1epq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epq
catalytic residue: ASP 215

1eprE02
type: Pdb
references: 1epr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epr
catalytic residue: ASP 215

1er8E02
type: Pdb
references: 1er8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1er8
catalytic residue: ASP 215

1gktA02
type: Pdb
references: 1gkt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gkt
catalytic residue: ASP 219

1gvtA02
type: Pdb
references: 1gvt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvt
catalytic residue: ASP 219

1gvuA02
type: Pdb
references: 1gvu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvu
catalytic residue: ASP 219

1gvvA02
type: Pdb
references: 1gvv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvv
catalytic residue: ASP 219

1gvwA02
type: Pdb
references: 1gvw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvw
catalytic residue: ASP 219

1gvxA02
type: Pdb
references: 1gvx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvx
catalytic residue: ASP 219

1od1A02
type: Pdb
references: 1od1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1od1
catalytic residue: ASP 219

1oewA02
type: Pdb
references: 1oew
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oew
catalytic residue: ASP 218

1oexA02
type: Pdb
references: 1oex
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oex
catalytic residue: ASP 218

2er0E02
type: Pdb
references: 2er0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er0
catalytic residue: ASP 215

2er6E02
type: Pdb
references: 2er6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er6
catalytic residue: ASP 215

2er7E02
type: Pdb
references: 2er7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er7
catalytic residue: ASP 215

2er9E02
type: Pdb
references: 2er9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er9
catalytic residue: ASP 215

3er3E02
type: Pdb
references: 3er3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3er3
catalytic residue: ASP 215

3er5E02
type: Pdb
references: 3er5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3er5
catalytic residue: ASP 215

4apeA02
type: Pdb
references: 4ape
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4ape
catalytic residue: ASP 215

4er1E02
type: Pdb
references: 4er1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4er1
catalytic residue: ASP 215

4er2E02
type: Pdb
references: 4er2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4er2
catalytic residue: ASP 215

4er4E02
type: Pdb
references: 4er4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4er4
catalytic residue: ASP 215

5er1E02
type: Pdb
references: 5er1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5er1
catalytic residue: ASP 215

5er2E02
type: Pdb
references: 5er2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5er2
catalytic residue: ASP 215

Analogue
compound: Peptide
pdb: 1e5oE01
ligand het code: 3AI

Analogue
compound: Peptide
pdb: 1er8E01
ligand het code: DHI-PRO-PHE-HIS-LEU-LEU-VAL-TYR (chain I)

Analogue
compound: Peptide
pdb: 1gvxA01
ligand het code: PRO-THR-GLU-PUK-ARG-GLU (chain I)

Analogue
compound: Peptide
pdb: 2er6E01
ligand het code: PRO-THR-GLU-PHE-PUK-ARG-GLU (chain I)

Analogue
compound: Peptide
pdb: 4er4E01
ligand het code: PRO-HIS-PRO-PHE-HIS-LAV-ILE-HIS-LYS (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1e80E01
ligand het code: 0GQ

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1e81E01
ligand het code: M91

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1e82E01
ligand het code: M90

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1eedP01
ligand het code: 0EO

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1entE01
ligand het code: 0EM

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1eplE01
ligand het code: PRO-LEU-GLU-PSA-ARG-LEU (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1epmE01
ligand het code: THR-PHE-GLN-ALA-PSA-LEU-ARG-GLU (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1epnE01
ligand het code: 2ZS

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1epoE01
ligand het code: 2Z3

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1eppE01
ligand het code: 1Z1

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1epqE01
ligand het code: 0QF

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1eprE01
ligand het code: 0QS

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1gktA01
ligand het code: BOC-HIS-PRO-PHE-HIS-LOV-ILE-HIS (chain B)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1gvtA01
ligand het code: 2ZS

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1gvuA01
ligand het code: PRO-PHE-HIS-STA-VAL-ILE (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1gvvA01
ligand het code: 0GM

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1gvwA01
ligand het code: 0EM

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1od1A01
ligand het code: 0QS

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1oexA01
ligand het code: BOC-HIS-PRO-PHE-ALA-LOV-ILE-HIS (chain B)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 2er0E01
ligand het code: IVA-HIS-PRO-PHE-HIS-CHS-LEU-PHE (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 2er7E01
ligand het code: BOC-HIS-PRO-PHE-HIS-LOV-ILE-HIS (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 2er9E01
ligand het code: BOC-HIS-PRO-PHE-HIS-STA-LEU-PHE (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 3er3E01
ligand het code: 0EL

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 3er5E01
ligand het code: PRO-HIS-PRO-PHE-HIS-STA-VAL-ILE-HIS-LYS (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 4er1E01
ligand het code: 0ZP

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 4er2E01
ligand het code: IVA-VAL-VAL-STA-ALA-STA (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 5er1E01
ligand het code: 0HT

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 5er2E01
ligand het code: 0EK

ReferenceForCatalyticMechanism
reference index: 6
reference section: Fig.3, p.11

ReferenceForCatalyticMechanism
reference index: 20
reference section: Fig.3, p.272

ReferenceForCatalyticMechanism
reference index: 24
reference section: Fig.4, p.325-326

ReferenceForCatalyticMechanism
reference index: 28
reference section: Fig.5

ReferenceForCatalyticMechanism
reference index: 29
reference section: Fig.2, Fig.7, Fig.8

ReferenceForCatalyticMechanism
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reference section: Fig.7

Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica.
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Energy calculations on aspartic proteinases: human renin, endothiapepsin and its complex with an angiotensinogen fragment analogue, H-142.
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The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
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Crystallographic studies of reduced bond inhibitors complexed with an aspartic proteinase.
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A Rational Approach to the Design of Antihypertensives. X-Ray Studies of Complexes between Aspartic Proteinases and Aminoalcohol Renin Inhibitors.
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X-ray studies of aspartic proteinase-statine inhibitor complexes.
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http://ezcatdb.cbrc.jp/EzCatDB/reference/D00441#13
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title: High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme.
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Comparative X-ray crystallographic evidence for a beta-bend conformation as the active structure for peptide T in T4 receptor recognition.
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Modulation of the affinity of aspartic proteases by the mutated residues in active site models.
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X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.
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Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution.
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X-ray analyses of aspartic proteinases. III Three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin at 1.6 A resolution.
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Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.
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X-ray analysis of a difluorostatone renin inhibitor bound as the tetrahedral hydrate to the aspartic protease endothiapepsin.
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A kinetic and equilibrium study of the denaturation of aspartic proteinases from the fungi, Endothia parasitica and Mucor miehei.
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X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors.
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Synthesis and crystallographic analysis of two rhizopuspepsin inhibitor complexes.
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Direct observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases.
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Domain flexibility in aspartic proteinases.
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Secondary substrate binding in aspartic proteinases: contributions of subsites S3 and S'2 to kcat.
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X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin.
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A quantum mechanical study of the active site of aspartic proteinases.
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Extending crystallographic information with semiempirical quantum mechanics and molecular mechanics: a case of aspartic proteinases.
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On the prediction of binding properties of drug molecules by comparative molecular field analysis.
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Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors.
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comment: X-ray crystallography
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A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica.
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Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin.
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A theoretical study of torsional flexibility in the active site of aspartic proteinases: implications for catalysis.
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The three-dimensional structure at 2.4 A resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae.
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A fast estimate of electrostatic group contributions to the free energy of protein-inhibitor binding.
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Refinement of Four Endothiapepsin Inhibitor Complexes. Crystallographic Studies of Cytochrome Ch from Methylobacterium Extorquens and Inhibitor Complexes of Aspartic Proteinases.
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Dynamic ligand design and combinatorial optimization: designing inhibitors to endothiapepsin.
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A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism.
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Five atomic resolution structures of endothiapepsin inhibitor complexes: implications for the aspartic proteinase mechanism.
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The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 A.
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Atomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides.
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comment: X-ray crystallography
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journal: Proteins
volume: 56
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title: Calculating proton uptake/release and binding free energy taking into account ionization and conformation changes induced by protein-inhibitor association: application to plasmepsin, cathepsin D and endothiapepsin-pepstatin complexes.

Endothia aspartic proteinase
type: KeggEnzyme

Endothia acid proteinase
type: KeggEnzyme

Endothia parasitica acid proteinase
type: KeggEnzyme

Endothia parasitica aspartic proteinase
type: KeggEnzyme