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3OF9

Structural Basis for Irreversible Inhibition of Human Cathepsin L by a Diazomethylketone 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 I0X A 501
ChainResidue
AARG9
AGLU64
AGLY68
AGLY69
ALEU70
AMET71
AALA136
AALA139
AMET162
AASP163
AHIS164
AGLU10
ATRP190
AGLU192
AGLY12
AGLN20
AGLY24
ASER25
ACYS26
ATRP27
AGLY62

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGqCGSCWAfSA
ChainResidueDetails
AGLN20-ALA31

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. MDHGVLVVGYG
ChainResidueDetails
AMET162-GLY172

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWgeeWGmgGYVkM
ChainResidueDetails
ATYR183-MET202

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:9468501
ChainResidueDetails
ACYS26

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AHIS164
AASN188

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:9468501
ChainResidueDetails
AGLU1

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN109

225946

PDB entries from 2024-10-09

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