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3CBJ

Chagasin-Cathepsin B complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0004869molecular_functioncysteine-type endopeptidase inhibitor activity
B0005515molecular_functionprotein binding
B0009986cellular_componentcell surface
B0020016cellular_componentciliary pocket
B0031410cellular_componentcytoplasmic vesicle
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 261
ChainResidue
ACYS62
APHE82
ALYS86
ALYS130
ATYR140
ALYS144

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 262
ChainResidue
ALYS127
ASER129
BASN110
AGLU57
AARG101
APRO126

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 111
ChainResidue
BGLU23
BHIS72
BHIS74

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 263
ChainResidue
AASN155
AASP227
ALYS232
ASER244

Functional Information from PROSITE/UniProt
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. YWLvANSWntdWGdnGFFkI
ChainResidueDetails
ATYR214-ILE233

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:9299326
ChainResidueDetails
AALA29
AHIS199
AASN219

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10605
ChainResidueDetails
ALYS141

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:3463996
ChainResidueDetails
AASN113

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 9pap
ChainResidueDetails
AHIS199
AASN219
AGLN23

221371

PDB entries from 2024-06-19

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