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- PDB-1pfh: THE PHOSPHORYLATED FORM OF THE HISTIDINE-CONTAINING PHOSPHOCARRIE... -

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Basic information

Entry
Database: PDB / ID: 1pfh
TitleTHE PHOSPHORYLATED FORM OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR
ComponentsPHOSPHO-HPR
KeywordsTRANSPORT PROTEIN / PHOSPHOCARRIER PROTEIN
Function / homology
Function and homology information


phosphotransferase activity, nitrogenous group as acceptor / antisigma factor binding / regulation of carbon utilization / positive regulation of glycogen catabolic process / phosphoenolpyruvate-dependent sugar phosphotransferase system / enzyme inhibitor activity / enzyme regulator activity / enzyme activator activity / cytosol
Similarity search - Function
Phosphotransferase system, HPr histidine phosphorylation site / PTS HPR domain histidine phosphorylation site signature. / Phosphotransferase system, HPr serine phosphorylation site / HPr-like / Phosphocarrier protein HPr-like / HPr-like superfamily / : / PTS HPr component phosphorylation site / PTS HPR domain profile. / Histidine-containing Protein; Chain: A; ...Phosphotransferase system, HPr histidine phosphorylation site / PTS HPR domain histidine phosphorylation site signature. / Phosphotransferase system, HPr serine phosphorylation site / HPr-like / Phosphocarrier protein HPr-like / HPr-like superfamily / : / PTS HPr component phosphorylation site / PTS HPR domain profile. / Histidine-containing Protein; Chain: A; / PTS HPR domain serine phosphorylation site signature. / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Phosphocarrier protein HPr
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR
AuthorsVan Nuland, N.A.J. / Scheek, R.M. / Robillard, G.T.
Citation
Journal: J.Mol.Biol. / Year: 1995
Title: High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data.
Authors: van Nuland, N.A. / Boelens, R. / Scheek, R.M. / Robillard, G.T.
#1: Journal: J.Mol.Biol. / Year: 1994
Title: The High-Resolution Structure of the Histidine-Containing Phosphocarrier Protein Hpr from Escherichia Coli Determined by Restrained Molecular Dynamics from Nuclear Magnetic Resonance Nuclear Overhauser Effect Data
Authors: Van Nuland, N.A.J. / Hangyi, I.W. / Van Schaik, R.C. / Berendsen, H.J.C. / Van Gunsteren, W.F. / Scheek, R.M. / Robillard, G.T.
#2: Journal: Nature / Year: 1993
Title: Active-Centre Torsion-Angle Strain Revealed in 1.6 Angstroms-Resolution Structure of Histidine-Containing Phosphocarrier Protein
Authors: Jia, Z. / Vandonselaar, M. / Quail, J.W. / Delbaere, L.T.J.
History
DepositionAug 18, 1995Processing site: BNL
Revision 1.0Nov 14, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Mar 26, 2025Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PHOSPHO-HPR


Theoretical massNumber of molelcules
Total (without water)9,2091
Polymers9,2091
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein PHOSPHO-HPR / P-HPR


Mass: 9209.312 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: PH 7.5, 20 DEGREES C, 50 MM KPI BUFFER / Source: (natural) Escherichia coli (E. coli) / Strain: HB2154 / References: UniProt: P0AA04
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other

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Processing

NMR softwareName: GROMOS / Developer: VAN GUNSTEREN,BERENDSEN / Classification: refinement
NMR ensembleConformers submitted total number: 20

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