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1EPL

A STRUCTURAL COMPARISON OF 21 INHIBITOR COMPLEXES OF THE ASPARTIC PROTEINASE FROM ENDOTHIA PARASITICA

Functional Information from GO Data
ChainGOidnamespacecontents
E0004190molecular_functionaspartic-type endopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PSA I 1
ChainResidue
ELEU120
EASP215
EGLY217
IGLU2
IARG2
ILEU3
EASP30
EASP32
EGLY34
ETYR75
EGLY76
EASP77
EPHE111

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR CHAIN I OF PS1, PRO-LEU-GLU-PSA-ARG-LEU
ChainResidue
EALA13
EASP77
EPHE189
EGLY217
ETHR218
ETHR219
EILE301
EHOH508
IPSA1
IGLU2
IARG2

site_idCAT
Number of Residues2
DetailsCATALYTIC RESIDUES
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 2024-09-18

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