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2XU3

CATHEPSIN L WITH A NITRILE INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE XU3 A 1221
ChainResidue
AGLN19
AGLY68
ALEU69
AMET70
AALA135
AMET161
AASP162
AHIS163
AGLY164
AALA214
ACL1223
AGLY23
AHOH2360
AHOH2366
ASER24
ACYS25
ATRP26
AGLY61
AGLU63
AASN66
AGLY67

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BTB A 1222
ChainResidue
AASN18
AGLY20
AGLN21
ALEU144
ATRP189
AHOH2361
AHOH2362
AHOH2364
AHOH2365

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1223
ChainResidue
AGLN19
AGLY23
AXU31221

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BTB A 1225
ChainResidue
ALYS117
AGLN118
AGLU119
AHOH2240
AHOH2367
AHOH2368
AHOH2370
AHOH2371
AHOH2372
AHOH2373

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGqCGSCWAfSA
ChainResidueDetails
AGLN19-ALA30

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. MDHGVLVVGYG
ChainResidueDetails
AMET161-GLY171

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWgeeWGmgGYVkM
ChainResidueDetails
ATYR182-MET201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:9468501
ChainResidueDetails
ACYS25

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AASN187
AHIS163

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN108

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PDB entries from 2024-06-12

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