SAXSdb — 3ezb

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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (PHOSPHOTRANSFER SYSTEM, ENZYME I)

Escherichia coli

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–259	Fragment：AMINO-TERMINAL DOMAIN RESIDUES 1 - 259	PROTEIN (PHOSPHOCARRIER PROTEIN HPR) × 1 （P0AA04）	SOLUTION NMR NMR measurement conditions：pH 7；313 K	Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 3EZB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1EZA AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE Deposited 1997-01-01	Different construct Different oligomeric state	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–258（258 aa） Fragment：AMINO-TERMINAL DOMAIN, RESIDUES 1 - 259	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided
1EZB AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 17 STRUCTURES Deposited 1997-01-01	Different construct Different oligomeric state	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–258（258 aa） Fragment：AMINO-TERMINAL DOMAIN, RESIDUES 1 - 259	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided
1EZC AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 17 STRUCTURES Deposited 1997-01-01	Different construct Different oligomeric state	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–258（258 aa） Fragment：AMINO-TERMINAL DOMAIN, RESIDUES 1 - 259	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided
1EZD AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI NMR, 16 STRUCTURES Deposited 1997-01-01	Different construct Different oligomeric state	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–258（258 aa） Fragment：AMINO-TERMINAL DOMAIN, RESIDUES 1 - 259	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided
1ZYM AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI Deposited 1996-05-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–258（258 aa） Fragment：AMINO-TERMINAL DOMAIN RESIDUES 1 - 258 Chain B 1–258（258 aa） Fragment：AMINO-TERMINAL DOMAIN RESIDUES 1 - 258	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.306
2EZA AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, RESTRAINED REGULARIZED MEAN STRUCTURE Deposited 1997-05-07	Different construct Different oligomeric state	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–258（258 aa） Fragment：AMINO-TERMINAL DOMAIN RESIDUES 1 - 259	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided
2EZB AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 14 STRUCTURES Deposited 1997-05-07	Different construct Different oligomeric state	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–258（258 aa） Fragment：AMINO-TERMINAL DOMAIN RESIDUES 1 - 259	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided
2EZC AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 14 STRUCTURES Deposited 1997-05-07	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–258（258 aa） Fragment：AMINO-TERMINAL DOMAIN RESIDUES 1 - 259	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.5；313 K	Resolution not provided
2HWG Structure of phosphorylated Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system Deposited 2006-08-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–575（575 aa） Chain B 1–575（575 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	MG MAGNESIUM ION × 2 OXL OXALATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；The protein sample (10 mg/mL) was mixed with MgCl2 and PEP to bring each additive to a final concentration of 10 mM. After ~5 min, sodium oxalate was added to a final concentration of 10 mM. Drops containing 1:1 protein and reservoir solution were equilibrated against reservoir solution containing 22% w/v polyethylene glycol 6000, 2% saturated ammonium sulfate, and 100 mM Na+HEPES., pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.70 Å R-free 0.284
2KX9 Solution Structure of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray Scattering Deposited 2010-04-29	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–573（573 aa） Fragment：UNP residues 1-573 Chain B 1–573（573 aa） Fragment：UNP residues 1-573	Not recorded	No recorded non-water small molecule	Experimental method not declared NMR measurement conditions pH 7.4；310 K；Pressure ambient NMR sample composition 20 mM TRIS, 100 mM sodium chloride, 10 mM DTT, 4 mM MgCl2, 1 mM EDTA, 10 % D2O, 1 tablet protease inhibitor, 0.15 mM EI dimer, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2L5H Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray Scattering Deposited 2010-11-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–573（573 aa） Chain B 1–573（573 aa）	Not recorded	No recorded non-water small molecule	Experimental method not declared NMR measurement conditions pH 7.4；310 K；Pressure ambient NMR sample composition 20 mM TRIS-1, 100 mM sodium chloride-2, 10 mM DTT-3, 4 mM MgCl2-4, 1 mM EDTA-5, 10 % D2O-6, 0.15 mM EI dimer-8, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2MP0 Protein Phosphorylation upon a Fleeting Encounter Deposited 2014-05-08	Different construct Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–258（258 aa） Fragment：N-terminal Domain, residues 1-258	Not recorded	PO3 PHOSPHITE ION × 1	SOLUTION NMR NMR measurement conditions pH 7.4；313.4 K NMR sample composition 0.5 mM [U-99% 15N] N-terminal Domain of Enzyme I-1, 0.5 mM [U-99% 15N] Enzyme II of Glucose-2, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1-14 mM [U-100% 1H; U-100% 12C; U-99%1 5N] N-terminal Domain of Enzyme I-3, 1-14 mM [U-99% 15N] EIN EIIAGlc-4, 1-14 mM EIN-5, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.4-1.5 mM [U-100% 2H; U-100% 12C; U-99% 15N] N-terminal Domain of Enzyme I-6, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2N5T Ensemble solution structure of the phosphoenolpyruvate-Enzyme I complex from the bacterial phosphotransferase system Deposited 2015-07-28	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–575（575 aa） Chain B 1–575（575 aa）	Not recorded	No recorded non-water small molecule	Experimental method not declared NMR measurement conditions pH 7.4；310 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition 0.4 mM [U-13C; U-15N; U-2H] EIA, 20 mM TRIS, 1 mM EDTA, 100 mM sodium chloride, 2 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2XDF Solution Structure of the Enzyme I Dimer Complexed with HPr Using Residual Dipolar Couplings and Small Angle X-Ray Scattering Deposited 2010-04-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–573（573 aa） Chain B 1–573（573 aa）	Not recorded	No recorded non-water small molecule	Experimental method not declared NMR measurement conditions pH 7.4；310 K；Pressure 1.0 NMR sample composition 90% H2O/10% D2O	Resolution not provided
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 Deposited 1998-11-03	Different construct	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–249（249 aa） Fragment：AMINO-TERMINAL DOMAIN RESIDUES 1 - 249	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided
3EZE COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE Deposited 1998-11-04	Different ligand/ion	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–259（259 aa） Fragment：AMINO-TERMINAL DOMAIN RESIDUES 1 - 259	Not recorded	PO3 PHOSPHITE ION × 1	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PT1_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–259； UniProt 1–259

PROTEIN (PHOSPHOCARRIER PROTEIN HPR)

Escherichia coli

UniProt P0AA04

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 1–85	Not recorded	PROTEIN (PHOSPHOTRANSFER SYSTEM, ENZYME I) × 1 （P08839）	SOLUTION NMR NMR measurement conditions：pH 7；313 K	Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 3EZB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CM2 STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES. Deposited 1999-05-13	Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Mutation：HIS15ASP	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.6	Resolution 1.80 Å
1CM3 HIS15ASP HPR FROM E. COLI Deposited 1999-05-13	Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Mutation：HIS15ASP	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.4；pH 5.4	Resolution 1.60 Å
1GGR COMPLEX OF ENZYME IIAGLC AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE Deposited 2000-09-18	Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Not recorded	PO3 PHOSPHITE ION × 1	SOLUTION NMR NMR measurement conditions pH 7.1；308 K；Ionic strength (raw mmCIF value) 10 mM SODIUM PHOSPHATE	Resolution not provided
1HDN THE HIGH-RESOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI DETERMINED BY RESTRAINED MOLECULAR DYNAMICS FROM NMR NUCLEAR OVERHAUSER EFFECT DATA Deposited 1994-02-10	Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1J6T COMPLEX OF ENZYME IIAMTL AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE Deposited 2002-08-14	Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Not recorded	PO3 PHOSPHITE ION × 1	SOLUTION NMR NMR measurement conditions pH 7；308 K；Ionic strength (raw mmCIF value) 10 mM SODIUM PHOSPHATE	Resolution not provided
1OPD HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED BY ASP (S46D) Deposited 1996-08-01	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Mutation：S46D	SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.50 Å R-free 0.234
1PFH THE PHOSPHORYLATED FORM OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR Deposited 1995-08-18	Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1POH THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR: A REDETERMINATION Deposited 1993-10-19	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
1VRC Complex of enzyme IIAmannose and the histidine-containing phosphocarrier protein HPr from escherichia coli nmr, restrained regularized mean structure Deposited 2005-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–85（85 aa） Chain D 1–85（85 aa）	Not recorded	PO3 PHOSPHITE ION × 2	SOLUTION NMR NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 40 mM SODIUM PHOSPHATE	Resolution not provided
2JEL JEL42 FAB/HPR COMPLEX Deposited 1998-02-24	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain P 1–85（85 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；pH 5.8	Resolution 2.50 Å R-free 0.280
2LRK Solution Structures of the IIA(Chitobiose)-HPr complex of the N,N'-Diacetylchitobiose Deposited 2012-04-06	Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 1–85（85 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.4；308 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient NMR sample composition 1.0 mM [U-100% 15N] HPr/IIAChb complex, 1.0 mM [U-100% 13C; U-100% 15N] HPR/IIAChb complex, 1.0 mM [U-100% 13C; U-100% 15N] HPR/IIAChb complex, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.0 mM [U-100% 15N] HPr/IIAChb complex, 1.0 mM [U-100% 13C; U-100% 15N] HPR/IIAChb complex, 1.0 mM [U-100% 13C; U-100% 15N] HPR/IIAChb complex, 100% D2O \| 100% D2O	Resolution not provided
2LRL Solution Structures of the IIA(Chitobiose)-HPr complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase System Deposited 2012-04-06	Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 1–85（85 aa）	Not recorded	PO3 PHOSPHITE ION × 1	SOLUTION NMR NMR measurement conditions pH 7.4；308 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient NMR sample composition 1.0 mM [U-99% 13C; U-99% 15N] protein, 1.0 mM D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
3CCD 1.0 A Structure of Post-Succinimide His15Asp HPr Deposited 2008-02-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–85（85 aa） Chain B 1–85（85 aa）	Mutation：His15Asp Mutation：His15Asp	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.4；287 K；0.1M citrate phosphate buffer, 25% saturated ammonium sulphate, pH 4.4, VAPOR DIFFUSION, HANGING DROP, temperature 287K	Resolution 1.00 Å R-free 0.205
3CCD 1.0 A Structure of Post-Succinimide His15Asp HPr Deposited 2008-02-25	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–85（85 aa）	Mutation：His15Asp	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.4；287 K；0.1M citrate phosphate buffer, 25% saturated ammonium sulphate, pH 4.4, VAPOR DIFFUSION, HANGING DROP, temperature 287K	Resolution 1.00 Å R-free 0.205
3CCD 1.0 A Structure of Post-Succinimide His15Asp HPr Deposited 2008-02-25	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–85（85 aa）	Mutation：His15Asp	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.4；287 K；0.1M citrate phosphate buffer, 25% saturated ammonium sulphate, pH 4.4, VAPOR DIFFUSION, HANGING DROP, temperature 287K	Resolution 1.00 Å R-free 0.205
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 Deposited 1998-11-03	Parsed fields agree	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided
3EZE COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE Deposited 1998-11-04	Different ligand/ion	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Not recorded	PO3 PHOSPHITE ION × 1	SOLUTION NMR NMR measurement conditions pH 7；313 K	Resolution not provided
4XWJ Histidine-containing phosphocarrier protein (HPr) and antisigma factor Rsd complex Deposited 2015-01-29	Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Mutation：F2S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；287.15 K；0.1 M NaCl, 0.1 M HEPES (pH 7.5), 1.6 M ammonium sulfate	Resolution 2.10 Å R-free 0.299
5YA0 Crystal structure of LsrK and HPr complex Deposited 2017-08-29	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–85（85 aa）	Not recorded	HEZ HEXANE-1,6-DIOL × 1 PO4 PHOSPHATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；5~20% (v/v) PEG-400, 0.1 M sodium phosphate-citrate (pH 4.2), and 0.2 M lithium sulfate	Resolution 3.00 Å R-free 0.239
5YA0 Crystal structure of LsrK and HPr complex Deposited 2017-08-29	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–85（85 aa）	Not recorded	HEZ HEXANE-1,6-DIOL × 1 PO4 PHOSPHATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；5~20% (v/v) PEG-400, 0.1 M sodium phosphate-citrate (pH 4.2), and 0.2 M lithium sulfate	Resolution 3.00 Å R-free 0.239
5YA1 crystal structure of LsrK-HPr complex with ATP Deposited 2017-08-29	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–85（85 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 HEZ HEXANE-1,6-DIOL × 2 PO4 PHOSPHATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；5~20% (v/v) PEG-400, 0.1M sodium phosphate-citrate (pH 4.2), 0.2M lithium sulfate	Resolution 2.70 Å R-free 0.254
5YA1 crystal structure of LsrK-HPr complex with ATP Deposited 2017-08-29	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–85（85 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 HEZ HEXANE-1,6-DIOL × 2 PO4 PHOSPHATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；5~20% (v/v) PEG-400, 0.1M sodium phosphate-citrate (pH 4.2), 0.2M lithium sulfate	Resolution 2.70 Å R-free 0.254
5YA2 Crystal structure of LsrK-HPr complex with ADP Deposited 2017-08-30	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–85（85 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 HEZ HEXANE-1,6-DIOL × 1 PO4 PHOSPHATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；5~20%(v/v) PEG-400, 0.1M sodium phosphate-citrate (pH 4.2), 0.2M lithium sulfate	Resolution 2.70 Å R-free 0.255
5YA2 Crystal structure of LsrK-HPr complex with ADP Deposited 2017-08-30	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–85（85 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 HEZ HEXANE-1,6-DIOL × 1 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；5~20%(v/v) PEG-400, 0.1M sodium phosphate-citrate (pH 4.2), 0.2M lithium sulfate	Resolution 2.70 Å R-free 0.255
6KCR X-ray structure of the MtlR-HPr complex from Escherichia coli Deposited 2019-06-28	Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–85（85 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289 K；100 mM Tris-HCl (pH 8.5), 200 mM Mg-acetate, 15% polyethylene glycol (PEG) 8000	Resolution 3.50 Å R-free 0.260
6KCR X-ray structure of the MtlR-HPr complex from Escherichia coli Deposited 2019-06-28	Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–85（85 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289 K；100 mM Tris-HCl (pH 8.5), 200 mM Mg-acetate, 15% polyethylene glycol (PEG) 8000	Resolution 3.50 Å R-free 0.260
9S8B Structure of glycogen phosphorylase - dimeric form - in complex with HPr from Escherichia coli Deposited 2025-08-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–85（85 aa） Chain D 1–85（85 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.79 Å
9S8K Structure of glycogen phosphorylase - tetrameric form - in complex with HPr from Escherichia coli Deposited 2025-08-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–85（85 aa） Chain F 1–85（85 aa） Chain G 1–85（85 aa） Chain H 1–85（85 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.06 Å

22 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PTHP_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–85； UniProt 1–85

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3ezb
Deposition date deposition_date	1998-11-03
Structure title title	COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI
Keywords keywords	PHOSPHOTRANSFERASE, KINASE, SUGAR TRANSPORT, TRANSFERASE; TRANSFERASE
Experimental Method method	SOLUTION NMR

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	24.14 Å
Radius of gyration Rg (electron density) rg_electron	24.02 Å
Forward intensity I(0) i0	30250100000.00
Molecular weight molecular_weight	1498000.0 kDa
Excluded volume excluded_volume	1882200 Å³
Envelope volume envelope_volume	97234 Å³
Hydration-shell volume shell_volume	30215 Å³
Envelope diameter envelope_diameter	102.4 Å
Shell Rg shell_rg	33.71 Å
Envelope Rg envelope_rg	28.99 Å
Shape Rg shape_rg	24.00 Å
Total Rg total_rg	24.14 Å
Total atoms total_atoms	212915
Residues n_residues	13759
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	85.4 Å
Rg (real space) rg_real	24.25 Å
Rg uncertainty (real space) rg_real_error	0.77 Å
I(0) (real space) i0_real	3.0250e+10
I(0) uncertainty (real space) i0_real_error	4.4250e+08
Rg (reciprocal space) rg_reciprocal	24.22 Å
I(0) (reciprocal space) i0_reciprocal	30250000000.0000
Solution quality estimate total_estimate	0.7737
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	24.0 Å
Skewness Skewness skewness	0.461
Kurtosis Kurtosis kurtosis	-0.195
Angular range angular_range	— – 0.3300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4185000.0000
Real-space data points n_real_points	65
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.745; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.821; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	PROTEIN (PHOSPHOTRANSFER SYSTEM, ENZYME I)
Molecular weight formula_weight	28381.3 kDa
EC 编号 ec_number	2.7.3.9
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	212916

MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDDEYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFITDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMRAVQEQVASEKAELAKLKDR

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	PROTEIN (PHOSPHOCARRIER PROTEIN HPR)
Molecular weight formula_weight	9129.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGKSASAKSLFKLQTLGLTQGTVVTISAEGEDEQKAVEHLVKLMAELE

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d3ezba1
Class class	a — All alpha proteins
Fold Fold fold	a.60 — SAM domain-like
Superfamily Superfamily superfamily	a.60.10 — Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain
Family Family family	a.60.10.1 — Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain

Domain ID domain_id	d3ezba2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.8 — The 'swivelling' beta/beta/alpha domain
Superfamily Superfamily superfamily	c.8.1 — Phosphohistidine domain
Family Family family	c.8.1.2 — N-terminal domain of enzyme I of the PEP:sugar phosphotransferase system

Domain ID domain_id	d3ezbb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.94 — HPr-like
Superfamily Superfamily superfamily	d.94.1 — HPr-like
Family Family family	d.94.1.1 — HPr-like

CATH v4.4 (3 domains)

Domain ID domain_id	3ezbA01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily	10 — Phosphohistidine domain

Domain ID domain_id	3ezbA02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	274 — Enzyme I; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — PtsI, HPr-binding domain

Domain ID domain_id	3ezbB00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1340 — Histidine-containing Protein; Chain: A;
Homologous superfamily homologous superfamily	10 — HPr-like

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8. Citations (4)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

fit	/app/data/saxs_computation/ez/3ezb/3ezb.fit
pddf	/app/data/pr_computation/ez/3ezb/3ezb.pr.out
profile	/app/data/saxs_computation/ez/3ezb/3ezb.dat

COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI

1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (PHOSPHOTRANSFER SYSTEM, ENZYME I)

State in the Current Structure

Other States of the Same Protein in the Database

PROTEIN (PHOSPHOCARRIER PROTEIN HPR)

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

8. Citations (4)

9. Files and Curves (10)

Files (7)

Curves (3)