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1EPQ

ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH PD-133,450 (SOT PHE GLY+SCC GCL)

Functional Information from GO Data
ChainGOidnamespacecontents
E0004190molecular_functionaspartic-type endopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 0QF E 327
ChainResidue
EASP12
EPHE189
EASP215
EGLY217
ETHR218
ETHR219
EILE297
EHOH589
EHOH591
EASP30
EASP32
EGLY34
ETYR75
EGLY76
EASP77
EPHE111
ELEU120

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 E 328
ChainResidue
ELYS238
ESER240
ESER241
ESER242
EHOH517

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 E 329
ChainResidue
ESER108
ESER109
ETHR319
EHOH452
EHOH500
EHOH505
EHOH538

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

220113

PDB entries from 2024-05-22

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