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Cocktail experiment C: fragments 103 and 171 in complex with Endothiapepsin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue DMS A 331
ChainResidue
ASER113
ASER114
ASER115

site_idAC2
Number of Residues2
Detailsbinding site for residue DMS A 332
ChainResidue
APRO26
AALA27

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 333
ChainResidue
ALYS330
AHOH1340
AHOH1581
AVAL272
ATYR277
AALA312
ASER329

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 334
ChainResidue
ASER297
AALA298
AGLY301
AILE302
AHOH867
AHOH1038

site_idAC5
Number of Residues7
Detailsbinding site for residue ACT A 335
ChainResidue
ACYS255
AASP279
APRO282
ACYS290
A46P336
AHOH1697
AHOH2095

site_idAC6
Number of Residues11
Detailsbinding site for residue 46P A 336
ChainResidue
ATYR163
AALA257
ATHR258
ALEU259
AGLY275
AASP276
AASP279
AACT335
AHOH1697
AHOH1962
AHOH2212

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. LDFDTGSSDLWV
ChainResidueDetails
ALEU32-VAL43
AGLY216-LEU227

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

243911

PDB entries from 2025-10-29

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