Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
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
DetailsACT_SITE:
ChainResidueDetails
ACYS73
AALA372
AASN396

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P70645
ChainResidueDetails
AMET1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS391

220113

PDB entries from 2024-05-22

PDB statisticsPDBj update infoContact PDBjnumon