Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1OPD

HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED BY ASP (S46D)

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 156
ChainResidue
AHOH108
AHIS15
ATHR16
AARG17
ALYS40
ASER41
AHOH107

site_idACT
Number of Residues2
DetailsTHE ACTIVE CENTER IS COMPOSED PRIMARILY OF TWO RESIDUES WHICH ARE CRITICAL IN PHOSPHOTRANSFER, HIS 15 AND ARG 17.
ChainResidue
AHIS15
AARG17

site_idAS6
Number of Residues1
DetailsIN GRAM-POSITIVE HPR HPRS PHOSPHOTRANSFER ABILITY CAN BE INHIBITED THROUGH PHOSPHORYLATION OF SER 46. WHILE SER 46 IS PRESENT IN GRAM-NEGATIVE HPRS THIS TYPE OF REGULATION IS NOT OF PHYSIOLOGICAL IMPORTANCE AS THE BACTERIA LACKS THE NECESSARY KINASE. IT IS POSSIBLE HOWEVER TO MIMIC THE REGULATORY PHOSPHORYLATION THROUGH THE MUTANT SER46ASP.
ChainResidue
AASP46

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

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

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon