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5HCT

Endothiapepsin in complex with biacylhydrazone

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue DMS A 401
ChainResidue
AASP81
AGLY221
ATHR222
ATHR223
A61P406
AHOH557

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 402
ChainResidue
ASER329
ALYS330
AHOH619
AVAL272
ATYR277
AALA312

site_idAC3
Number of Residues9
Detailsbinding site for residue GOL A 403
ChainResidue
ASER297
AALA298
AGLY301
AILE302
AASN303
AHOH502
AHOH506
AHOH607
AHOH660

site_idAC4
Number of Residues5
Detailsbinding site for residue ACT A 405
ChainResidue
ACYS255
AASP279
AGLY281
ACYS290
AHOH588

site_idAC5
Number of Residues13
Detailsbinding site for residue 61P A 406
ChainResidue
AASP33
AASP35
ATYR79
AGLY80
AASP81
ASER83
AASP219
AGLY221
ATHR222
ATYR226
AILE300
ADMS401
AHOH540

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 407
ChainResidue
AALA187
ATHR198
AASP215

site_idAC7
Number of Residues3
Detailsbinding site for residue PG4 A 408
ChainResidue
AASP15
APHE280
AILE283

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

239492

PDB entries from 2025-07-30

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