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1CM2

STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004857molecular_functionenzyme inhibitor activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008047molecular_functionenzyme activator activity
A0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
A0016775molecular_functionphosphotransferase activity, nitrogenous group as acceptor
A0030234molecular_functionenzyme regulator activity
A0043609biological_processregulation of carbon utilization
A0045152molecular_functionantisigma factor binding
A0045819biological_processpositive regulation of glycogen catabolic process
A0071702biological_processorganic substance transport
Functional Information from PROSITE/UniProt
site_idPS00589
Number of Residues16
DetailsPTS_HPR_SER PTS HPR domain serine phosphorylation site signature. GKsASaKSLFKLQtLG
ChainResidueDetails
AGLY39-GLY54

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Pros-phosphohistidine intermediate => ECO:0000255|PROSITE-ProRule:PRU00681, ECO:0000269|PubMed:2261470
ChainResidueDetails
AASP15

218853

PDB entries from 2024-04-24

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