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6AY2

Structure of CathB with covalently linked Compound 28

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 Residues9
Detailsbinding site for residue C1G A 301
ChainResidue
AGLN23
AGLY27
ACYS29
ATRP30
AGLY73
AGLY74
AGLY198
AHIS199
ATHR223

site_idAC2
Number of Residues14
Detailsbinding site for residue C1G B 301
ChainResidue
BGLN23
BGLY27
BSER28
BTRP30
BALA31
BPHE32
BGLY33
BGLY73
BGLY74
BPRO76
BGLY198
BHIS199
BALA200
BTHR223

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. YWLvANSWntdWGdnGFFkI
ChainResidueDetails
ATYR214-ILE233

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:9299326
ChainResidueDetails
ACYS29
AHIS199
AASN219
BCYS29
BHIS199
BASN219

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10605
ChainResidueDetails
ALYS141
BLYS141

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:3463996
ChainResidueDetails
AASN113
BASN113

221051

PDB entries from 2024-06-12

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