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2ER0

X-RAY STUDIES OF ASPARTIC PROTEINASE-STATINE INHIBITOR COMPLEXES

Functional Information from GO Data
ChainGOidnamespacecontents
E0004190molecular_functionaspartic-type endopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR CHAIN I OF L364,099
ChainResidue
ETYR75
EGLY76
EASP77
EPHE111
EASP114
EILE117
ELEU120
EASP215
EGLY217
ETHR218
ETHR219
EILE278
EILE297
EILE301
ELEU10
EASP12
EALA13
EASP30
EASP32
EGLY34
ESER74

site_idCAT
Number of Residues2
Details
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 Residues311
DetailsDomain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {}
ChainResidueDetails

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

238895

건을2025-07-16부터공개중

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