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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
A0036525biological_processprotein deglycation
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
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14500888","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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