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3EZA

COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE

Functional Information from GO Data
ChainGOidnamespacecontents
A0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
A0016310biological_processphosphorylation
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0004857molecular_functionenzyme inhibitor activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008047molecular_functionenzyme activator activity
B0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
B0016775molecular_functionphosphotransferase activity, nitrogenous group as acceptor
B0030234molecular_functionenzyme regulator activity
B0043609biological_processregulation of carbon utilization
B0045152molecular_functionantisigma factor binding
B0045819biological_processpositive regulation of glycogen catabolic process
Functional Information from PROSITE/UniProt
site_idPS00369
Number of Residues8
DetailsPTS_HPR_HIS PTS HPR domain histidine phosphorylation site signature. GLHTRPAA
ChainResidueDetails
BGLY13-ALA20

site_idPS00370
Number of Residues12
DetailsPEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGrTsHTSIMAR
ChainResidueDetails
AGLY184-ARG195

site_idPS00589
Number of Residues16
DetailsPTS_HPR_SER PTS HPR domain serine phosphorylation site signature. GKsASaKSLFKLQtLG
ChainResidueDetails
BGLY39-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
BHIS15

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1zym
ChainResidueDetails
AHIS189
ATHR168

site_idMCSA1
Number of Residues1
DetailsM-CSA 920
ChainResidueDetails
AHIS189covalent catalysis

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PDB entries from 2024-07-24

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