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1EPP

ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH PD-130,693 (MAS PHE LYS+MTF STA MBA)

Functional Information from GO Data
ChainGOidnamespacecontents
E0004190molecular_functionaspartic-type endopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 E 327
ChainResidue
ELYS238
ESER240
ESER241
ESER242
EHOH521

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 E 328
ChainResidue
EHOH459
EHOH542
ESER108
ESER109
ETHR318
ETHR319

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 1Z1 E 333
ChainResidue
EASP12
EASP30
EASP32
EGLY34
ETYR75
EGLY76
EASP77
EASP114
EPHE189
EASP215
EGLY217
ETHR218
ETHR219
EHOH335

site_idCAT
Number of Residues2
DetailsCATALYTIC SITE
ChainResidue
EASP32
EASP215

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. LDFDTGSSDLWV
ChainResidueDetails
ELEU29-VAL40
EGLY212-LEU223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
EASP32
ESER194

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP32

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP215

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP215
ESER35
ETHR218
EASP32

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP215
ETHR216
EASP32
ETHR33

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP215
ESER35
EASP32

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP215
ETHR218
EASP32
ETHR33

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PDB entries from 2024-07-17

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