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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P08839 New Search
17PDB entries
17Biological assembly
23chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1EZA AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE Deposited 1997-01-01 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 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 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–573（573 aa）
Chain B 1–573（573 aa）
Not recorded No recorded non-water small molecule 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 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–575（575 aa）
Chain B 1–575（575 aa）
Not recorded No recorded non-water small molecule 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 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–573（573 aa）
Chain B 1–573（573 aa）
Not recorded No recorded non-water small molecule 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 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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
3EZB COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI Deposited 1998-11-03 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–259（259 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
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.