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4BSQ

MOUSE CATHEPSIN S WITH COVALENT LIGAND

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE QQV A 1341
ChainResidue
AGLN141
AVAL285
AASN286
AHIS287
ATYR334
AGLY145
ACYS147
ATRP148
ALYS187
AGLY191
AGLY192
ATYR193
AGLY260

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1342
ChainResidue
ALYS248
AARG323
AASN324
AHOH2003
AHOH2111

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1343
ChainResidue
AGLU181
AGLU182
AHOH2054

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1344
ChainResidue
ALYS187
ATHR282
AGLY283
AHOH2059
AHOH2136
AHOH2161

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1345
ChainResidue
AGLN199
AILE202
AHOH2067
AHOH2072

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGACWAfSA
ChainResidueDetails
AGLN141-ALA152

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VNHGVLVVGYG
ChainResidueDetails
AVAL285-GLY295

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWglnFGdqGYIrM
ChainResidueDetails
ATYR302-MET321

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ACYS147
AHIS287
AASN307

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN120

222415

PDB entries from 2024-07-10

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