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1MHW

Design of non-covalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
C0006508biological_processproteolysis
C0008234molecular_functioncysteine-type peptidase activity
D0006508biological_processproteolysis
D0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DAR E 43P
ChainResidue
AGLN21
BHOH785
ECYS42
EHOH497

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DAR F 43P
ChainResidue
AHOH494
AHOH704
BGLN21
FCYS42
FHOH797

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DAR G 43P
ChainResidue
AARG8
AGLU9
AGLY11
ACSD25
AGLY67
AGLY68
AASP162
AHOH704
GCYS42
GTYR44

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE DAR H 43P
ChainResidue
BCSD25
BTRP26
BGLY67
BGLY68
BGLN78
BASP79
BGLY81
BMET161
BASP162
HCYS42
HTYR44
HPEA45
HHOH458
HHOH631

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
CTYR182-MET201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
CASN187
DASN187

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AHIS163
BHIS163

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN108
BASN108

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 8pch
ChainResidueDetails
AGLN19
AHIS163

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 8pch
ChainResidueDetails
BGLN19
BHIS163

224201

PDB entries from 2024-08-28

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