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5RBQ

PanDDA analysis group deposition -- Endothiapepsin changed state model for fragment F2X-Entry Library B06b

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue R8P A 401
ChainResidue
AASP33
AHOH508
AHOH510
AHOH599
AHOH684
AHOH719
AASP35
ATYR79
AASP81
ASER83
ASER115
APHE116
ALEU125
AGLY221

site_idAC2
Number of Residues5
Detailsbinding site for residue DMS A 402
ChainResidue
AASP81
AGLY221
ATHR222
ATHR223
AHOH555

site_idAC3
Number of Residues6
Detailsbinding site for residue DMS A 403
ChainResidue
AASP81
AGLY82
ASER83
ASER113
ASER114
ASER115

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 404
ChainResidue
AALA237
AGLN238
ASER240
AGOL409
AHOH518

site_idAC5
Number of Residues5
Detailsbinding site for residue DMS A 405
ChainResidue
AVAL204
AGLY205
ASER206
AGLY207
AGLN238

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 406
ChainResidue
ALEU69
ASER71
ATYR179
AGLY181
ASER182
AGLY286
AHOH540

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL A 407
ChainResidue
AVAL272
APRO274
ATYR277
AALA312
ASER329
ALYS330
AHOH637

site_idAC8
Number of Residues9
Detailsbinding site for residue GOL A 408
ChainResidue
ASER297
AALA298
AGLY301
AILE302
AASN303
AHOH502
AHOH536
AHOH560
AHOH646

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL A 409
ChainResidue
AVAL239
AGLY241
AALA242
AGOL404
AHOH501
AHOH515
AHOH518

site_idAD1
Number of Residues7
Detailsbinding site for residue ACT A 410
ChainResidue
ACYS255
AASP279
AGLY281
APRO282
ACYS290
AHOH519
AHOH597

site_idAD2
Number of Residues4
Detailsbinding site for residue PG4 A 411
ChainResidue
AASP15
APHE280
AILE283
ANA412

site_idAD3
Number of Residues1
Detailsbinding site for residue NA A 412
ChainResidue
APG4411

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 Residues2
DetailsACT_SITE:
ChainResidueDetails
AASP35
ASER199

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PDB entries from 2024-06-12

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