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1CTE

CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN

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 Residues8
DetailsBINDING SITE FOR RESIDUE PYS A 255
ChainResidue
AHIS199
AALA200
AILE201
AASN219
ATRP221
AGLN23
ACYS29
APHE180

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PYS B 255
ChainResidue
BGLN23
BCYS29
BPHE174
BVAL176
BHIS199
BALA200
BILE201
BASN219
BTRP221
BHOH757

site_idACT
Number of Residues3
DetailsACTIVE SITE RESIDUES FOR RAT CATHEPSIN B IN CHAIN A
ChainResidue
ACYS29
AHIS199
AASN219

site_idBCT
Number of Residues3
DetailsACTIVE SITE RESIDUES FOR RAT CATHEPSIN B IN CHAIN B
ChainResidue
BCYS29
BHIS199
BASN219

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_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EAGDVMGGHAI
ChainResidueDetails
AGLU191-ILE201

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. GGHAIRILGWG
ChainResidueDetails
AGLY197-GLY207

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvANSWnadWGdnGFFkI
ChainResidueDetails
ATYR214-ILE233

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000269|PubMed:7890671, ECO:0000269|PubMed:8740363
ChainResidueDetails
ACYS29
BCYS29

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089, ECO:0000269|PubMed:7890671, ECO:0000269|PubMed:8740363
ChainResidueDetails
AHIS199
BHIS199

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090, ECO:0000269|PubMed:7890671, ECO:0000269|PubMed:8740363
ChainResidueDetails
AASN219
BASN219

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10605
ChainResidueDetails
ALYS141
BLYS141

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:6574504
ChainResidueDetails
AASN113
BASN113

218853

PDB entries from 2024-04-24

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