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2DCD

X-ray crystal structure analysis of bovine spleen cathepsin B-CA078 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 801
ChainResidue
APRO2
AGLN10
ASER129
ATYR165
AHOH833
AHOH892

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 78A A 780
ChainResidue
ASER28
ACYS29
ATRP30
AGLY73
AGLY74
AHIS110
AHIS111
AGLY121
AALA173
AGLY198
AHIS199
ATRP221
AGLU245
AHOH901
AGLN23
AGLY24
AGLY27

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 500
ChainResidue
AARG8
ALEU216
AASP227
AASN228
ALYS232

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
AGLY197-GLY207

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000269|PubMed:10739956, ECO:0000269|PubMed:7106283
ChainResidueDetails
ACYS29

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089, ECO:0000269|PubMed:10739956
ChainResidueDetails
AHIS199

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090, ECO:0000269|PubMed:10739956
ChainResidueDetails
AASN219

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10605
ChainResidueDetails
ALYS141

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:3379063
ChainResidueDetails
AASN113

219140

PDB entries from 2024-05-01

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