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1SP4

Crystal structure of NS-134 in complex with bovine cathepsin B: a two headed epoxysuccinyl inhibitor extends along the whole active site cleft

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE EP2 B 48
ChainResidue
AGLN23
BHIS110
BHIS111
BALA173
BALA173
BPHE174
BSER175
BGLY198
BHIS199
BTRP221
BGLY241
AGLY24
BSER244
BGLU245
BHOH291
BHOH327
BHOH354
AGLY27
ASER28
ACYS29
ATRP30
BGLY73
BGLY74
BPRO76

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGSCWAfGA
ChainResidueDetails
AGLN23-ALA34

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. GGHAIRILGWG
ChainResidueDetails
BGLY197-GLY207

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvGNSWntdWGdnGFFkI
ChainResidueDetails
BTYR214-ILE233

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089, ECO:0000269|PubMed:10739956
ChainResidueDetails
BHIS199

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090, ECO:0000269|PubMed:10739956
ChainResidueDetails
BASN219

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10605
ChainResidueDetails
BLYS141

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:3379063
ChainResidueDetails
BASN113

222415

PDB entries from 2024-07-10

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