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1POH

THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR: A REDETERMINATION

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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 90
ChainResidue
AHIS15
ATHR16
AARG17
ALYS40
ASER41
AHOH113
AHOH136

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 91
ChainResidue
ALYS40
AHOH130
AHOH168
ALYS27
AASN38

Functional Information from PROSITE/UniProt
site_idPS00369
Number of Residues8
DetailsPTS_HPR_HIS PTS HPR domain histidine phosphorylation site signature. GLHTRPAA
ChainResidueDetails
AGLY13-ALA20

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
AHIS15

226707

PDB entries from 2024-10-30

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