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7V5L

Crystal structure of human bleomycin hydrolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0004177molecular_functionaminopeptidase activity
A0004180molecular_functioncarboxypeptidase activity
A0004197molecular_functioncysteine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0009410biological_processresponse to xenobiotic stimulus
A0009636biological_processresponse to toxic substance
A0016787molecular_functionhydrolase activity
A0042802molecular_functionidentical protein binding
A0043418biological_processhomocysteine catabolic process
A0070005molecular_functioncysteine-type aminopeptidase activity
A0070062cellular_componentextracellular exosome
B0000209biological_processprotein polyubiquitination
B0004177molecular_functionaminopeptidase activity
B0004180molecular_functioncarboxypeptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008234molecular_functioncysteine-type peptidase activity
B0009410biological_processresponse to xenobiotic stimulus
B0009636biological_processresponse to toxic substance
B0016787molecular_functionhydrolase activity
B0042802molecular_functionidentical protein binding
B0043418biological_processhomocysteine catabolic process
B0070005molecular_functioncysteine-type aminopeptidase activity
B0070062cellular_componentextracellular exosome
C0000209biological_processprotein polyubiquitination
C0004177molecular_functionaminopeptidase activity
C0004180molecular_functioncarboxypeptidase activity
C0004197molecular_functioncysteine-type endopeptidase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008234molecular_functioncysteine-type peptidase activity
C0009410biological_processresponse to xenobiotic stimulus
C0009636biological_processresponse to toxic substance
C0016787molecular_functionhydrolase activity
C0042802molecular_functionidentical protein binding
C0043418biological_processhomocysteine catabolic process
C0070005molecular_functioncysteine-type aminopeptidase activity
C0070062cellular_componentextracellular exosome
D0000209biological_processprotein polyubiquitination
D0004177molecular_functionaminopeptidase activity
D0004180molecular_functioncarboxypeptidase activity
D0004197molecular_functioncysteine-type endopeptidase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008234molecular_functioncysteine-type peptidase activity
D0009410biological_processresponse to xenobiotic stimulus
D0009636biological_processresponse to toxic substance
D0016787molecular_functionhydrolase activity
D0042802molecular_functionidentical protein binding
D0043418biological_processhomocysteine catabolic process
D0070005molecular_functioncysteine-type aminopeptidase activity
D0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QKsSGRCWIfSC
ChainResidueDetails
AGLN67-CYS78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE:
ChainResidueDetails
ACYS73
DCYS73
DHIS372
DASN396
AHIS372
AASN396
BCYS73
BHIS372
BASN396
CCYS73
CHIS372
CASN396

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P70645
ChainResidueDetails
AMET1
BMET1
CMET1
DMET1

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS391
BLYS391
CLYS391
DLYS391

237735

PDB entries from 2025-06-18

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