Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2XU4

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 Residues22
DetailsBINDING SITE FOR RESIDUE DJT A 1221
ChainResidue
AARG8
AGLY67
AGLY68
ALEU69
AMET70
AALA135
AMET161
AASP162
AHIS163
AGLY164
AALA214
AGLU9
AGOL1222
AHOH2096
AHOH2250
AGLY11
AGLN19
AGLY23
ASER24
ACYS25
ATRP26
AGLU63

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1222
ChainResidue
AASP162
AHIS163
AGLU191
AGLY196
ADJT1221
AHOH2218
AHOH2223
AHOH2251
AHOH2252

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 1223
ChainResidue
AASN18

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
AHIS163
AASN187

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

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon