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1ONS

Crystal structure of Escherichia coli heat shock protein YedU

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006974biological_processDNA damage response
A0008270molecular_functionzinc ion binding
A0010447biological_processresponse to acidic pH
A0016787molecular_functionhydrolase activity
A0016790molecular_functionthiolester hydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0016829molecular_functionlyase activity
A0019172molecular_functionglyoxalase III activity
A0019243biological_processmethylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
A0019249biological_processlactate biosynthetic process
A0030091biological_processprotein repair
A0036524molecular_functionprotein deglycase activity
A0042245biological_processRNA repair
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0051595biological_processresponse to methylglyoxal
A0106044biological_processguanine deglycation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 451
ChainResidue
AHIS85
AHIS85
AGLU90
AGLU90
AHIS122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305
ChainResidueDetails
AHIS185

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:14500888
ChainResidueDetails
AALA86
APHE91
ALYS123

218853

PDB entries from 2024-04-24

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