SAXSdb — 2mp0

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

Phosphoenolpyruvate-protein phosphotransferase

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 1–258	Fragment：N-terminal Domain, residues 1-258	Glucose-specific phosphotransferase enzyme IIA component × 1 （P69783） 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

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 2MP0	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 Different ligand/ion 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；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 Different ligand/ion 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；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 Different ligand/ion 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；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 Different ligand/ion 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；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 ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–258（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 Different ligand/ion 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；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 Different ligand/ion 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；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 ligand/ion 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 ligand/ion 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 ligand/ion 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
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 ligand/ion 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 ligand/ion 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 Different ligand/ion Different experimental conditions	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
3EZB COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI Deposited 1998-11-03	Different construct Different ligand/ion Different experimental conditions	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	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 construct Different experimental conditions	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 1–258； UniProt 1–258

Glucose-specific phosphotransferase enzyme IIA component

Escherichia coli

UniProt P69783

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 2–169	Not recorded	Phosphoenolpyruvate-protein phosphotransferase × 1 （P08839） 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

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 2MP0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1F3G THREE-DIMENSIONAL STRUCTURE OF THE ESCHERICHIA COLI PHOSPHOCARRIER PROTEIN III GLC Deposited 1991-08-28	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 8–168（161 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å
1F3Z IIAGLC-ZN COMPLEX Deposited 1997-10-09	Different construct 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 8–168（161 aa）	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；0.1-0.3 M SODIUM ACETATE, 1MM ZINC ACETATE, 0.1 M TRIS BUFFER PH 8.5	Resolution 1.98 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 construct Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–168（168 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
1GLA STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE Deposited 1992-10-28	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain F 1–168（168 aa）	Not recorded	GOL GLYCEROL × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
1GLB STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE Deposited 1992-10-28	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain F 1–168（168 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 4 GOL GLYCEROL × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
1GLC CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROTEIN IS CONTROLLED BY PHOSPHORYLATION Deposited 1994-03-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain F 1–168（168 aa）	Not recorded	ZN ZINC ION × 4 MG MAGNESIUM ION × 4 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.65 Å
1GLC CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROTEIN IS CONTROLLED BY PHOSPHORYLATION Deposited 1994-03-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain F 1–168（168 aa）	Not recorded	ZN ZINC ION × 2 MG MAGNESIUM ION × 2 G3H GLYCERALDEHYDE-3-PHOSPHATE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.65 Å
1GLC CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROTEIN IS CONTROLLED BY PHOSPHORYLATION Deposited 1994-03-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain F 1–168（168 aa）	Not recorded	ZN ZINC ION × 2 MG MAGNESIUM ION × 2 G3H GLYCERALDEHYDE-3-PHOSPHATE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.65 Å
1GLD CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROTEIN IS CONTROLLED BY PHOSPHORYLATION Deposited 1994-03-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain F 1–168（168 aa）	Not recorded	MN MANGANESE (II) ION × 4 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.93 Å
1GLE CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROTEIN IS CONTROLLED BY PHOSPHORYLATION Deposited 1994-03-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain F 1–168（168 aa）	Not recorded	ZN ZINC ION × 8 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.94 Å
1GLE CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROTEIN IS CONTROLLED BY PHOSPHORYLATION Deposited 1994-03-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain F 1–168（168 aa）	Not recorded	ZN ZINC ION × 4 G3H GLYCERALDEHYDE-3-PHOSPHATE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.94 Å
1GLE CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROTEIN IS CONTROLLED BY PHOSPHORYLATION Deposited 1994-03-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain F 1–168（168 aa）	Not recorded	ZN ZINC ION × 4 G3H GLYCERALDEHYDE-3-PHOSPHATE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.94 Å
1O2F COMPLEX OF ENZYME IIAGLC AND IIBGLC PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE Deposited 2003-03-11	Different construct Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–168（168 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
2F3G IIAGLC CRYSTAL FORM III Deposited 1997-10-14	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 1–168（168 aa） Chain B 1–168（168 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；30% PEG 4000, 0.2M MGCL2, 0.1M TRIS, PH 8.5 4 DEGREES	Resolution 2.13 Å
4JBW Crystal structure of E. coli maltose transporter MalFGK2 in complex with its regulatory protein EIIAglc Deposited 2013-02-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain M 1–169（169 aa） Chain N 1–169（169 aa）	Not recorded	PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；295 K；13% PEG monomethylether 2000, 100mM Sodium cacodylate pH 5.6, 100mM Non Detergent Sulfobetaine (NDSB-256), VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 3.91 Å R-free 0.281
4JBW Crystal structure of E. coli maltose transporter MalFGK2 in complex with its regulatory protein EIIAglc Deposited 2013-02-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain O 1–169（169 aa） Chain P 1–169（169 aa）	Not recorded	PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；295 K；13% PEG monomethylether 2000, 100mM Sodium cacodylate pH 5.6, 100mM Non Detergent Sulfobetaine (NDSB-256), VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 3.91 Å R-free 0.281

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

View Construct and Data Evidence

UniProt name	PTGA_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–168； UniProt 2–169

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	2mp0
Deposition date deposition_date	2014-05-08
Structure title title	Protein Phosphorylation upon a Fleeting Encounter
Keywords keywords	EIN EIIAGlc complex, 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	24.99 Å
Radius of gyration Rg (electron density) rg_electron	24.08 Å
Forward intensity I(0) i0	31139600.00
Molecular weight molecular_weight	43251.0 kDa
Excluded volume excluded_volume	54569 Å³
Envelope volume envelope_volume	69937 Å³
Hydration-shell volume shell_volume	25054 Å³
Envelope diameter envelope_diameter	82.8 Å
Shell Rg shell_rg	30.25 Å
Envelope Rg envelope_rg	24.20 Å
Shape Rg shape_rg	24.05 Å
Total Rg total_rg	24.96 Å
Total atoms total_atoms	6156
Residues n_residues	398
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	83.4 Å
Rg (real space) rg_real	24.95 Å
Rg uncertainty (real space) rg_real_error	0.47 Å
I(0) (real space) i0_real	3.1140e+07
I(0) uncertainty (real space) i0_real_error	4.3320e+05
Rg (reciprocal space) rg_reciprocal	24.97 Å
I(0) (reciprocal space) i0_reciprocal	31140000.0000
Solution quality estimate total_estimate	0.8905
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	26.5 Å
Skewness Skewness skewness	0.258
Kurtosis Kurtosis kurtosis	-0.516
Angular range angular_range	— – 0.3200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	8892000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.996

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Phosphoenolpyruvate-protein phosphotransferase
Molecular weight formula_weight	28224.1 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	6156

MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDDEYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFITDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMRAVQEQVASEKAELAKLKD

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	83333
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Glucose-specific phosphotransferase enzyme IIA component
Molecular weight formula_weight	18141.8 kDa
EC 编号 ec_number	2.7.1.-
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

GLFDKLKSLVSDDKKDTGTIEIIAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMVAPVDGTIGKIFETNHAFSIESDSGVELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDTVIEFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	83333
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	PHOSPHITE ION
Molecular weight formula_weight	79.0 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2mp0b_
Class class	b — All beta proteins
Fold Fold fold	b.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamily	b.84.3 — Duplicated hybrid motif
Family Family family	b.84.3.1 — Glucose permease-like

CATH v4.4 (3 domains)

Domain ID domain_id	2mp0A01
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	2mp0A02
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	2mp0B00
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	70 — Glucose Permease (Domain IIA)
Homologous superfamily homologous superfamily	10 — Glucose Permease (Domain IIA)

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8. Citations (2)

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fit	/app/data/saxs_computation/mp/2mp0/2mp0.fit
pddf	/app/data/pr_computation/mp/2mp0/2mp0.pr.out
profile	/app/data/saxs_computation/mp/2mp0/2mp0.dat

Protein Phosphorylation upon a Fleeting Encounter

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

Phosphoenolpyruvate-protein phosphotransferase

State in the Current Structure

Other States of the Same Protein in the Database

Glucose-specific phosphotransferase enzyme IIA component

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

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

CATH v4.4 (3 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)