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7XF9

Crystal structure of human bleomycin hydrolase H372A mutant

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
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 Residues3
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P70645","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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