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1aqt

EPSILON SUBUNIT OF F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI

Method: X-RAY DIFFRACTION Dmax: 60.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ATP SYNTHASE

Escherichia coli

UniProt P0A6E6

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 3–138 Fragment：EPSILON CHAIN Mutation：A1G, M2S No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；PROTEIN (4 MG/ML)IN 50 MM HEPES BUFFER, PH 7.5, 200 MM (NH2)2SO4, 2 M (NA/K)PO4 Resolution 2.30 Å R-free 0.288

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 1AQT Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BSH SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX Deposited 1998-08-27 Different construct 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 1–138（138 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；295 K；Ionic strength (raw mmCIF value) 0.03；Pressure 10000
Resolution not provided
1BSN SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX Deposited 1998-08-28 Different construct 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 1–138（138 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；295 K；Ionic strength (raw mmCIF value) 0.03；Pressure 10000
Resolution not provided
1FS0 COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI Deposited 2000-09-07 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 1–138（138 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；298 K；0.5M tartrate, pH 8.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.10 Å R-free 0.269
1FS0 COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI Deposited 2000-09-07 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain E 1–138（138 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；298 K；0.5M tartrate, pH 8.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.10 Å R-free 0.269

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPE_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–138； UniProt 3–138

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1aqt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1aqt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1aqt
Deposition date deposition_date1997-07-31
Structure title titleEPSILON SUBUNIT OF F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI
Keywords keywordsHYDROLASE, ATPASE, ATP SYNTHASE, EPSILON SUBUNIT; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.33 Å
Radius of gyration Rg (electron density) rg_electron16.16 Å
Forward intensity I(0) i04225180.00
Molecular weight molecular_weight14597.0 kDa
Excluded volume excluded_volume18267 ų
Envelope volume envelope_volume21646 ų
Hydration-shell volume shell_volume12162 ų
Envelope diameter envelope_diameter61.6 Å
Shell Rg shell_rg20.90 Å
Envelope Rg envelope_rg16.46 Å
Shape Rg shape_rg16.20 Å
Total Rg total_rg16.96 Å
Total atoms total_atoms1027
Residues n_residues135
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax60.9 Å
Rg (real space) rg_real17.39 Å
Rg uncertainty (real space) rg_real_error0.51 Å
I(0) (real space) i0_real4.2250e+06
I(0) uncertainty (real space) i0_real_error5.7280e+04
Rg (reciprocal space) rg_reciprocal17.38 Å
I(0) (reciprocal space) i0_reciprocal4225000.0000
Solution quality estimate total_estimate0.7705
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.0 Å
Skewness Skewness skewness0.449
Kurtosis Kurtosis kurtosis-0.150
Angular range angular_range— – 0.4600 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha615400.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.706; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.899; 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)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1aqta1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.10 — Epsilon subunit of F1F0-ATP synthase C-terminal domain
Family Family familya.2.10.1 — Epsilon subunit of F1F0-ATP synthase C-terminal domain
Domain ID domain_idd1aqta2
Class classb — All beta proteins
Fold Fold foldb.93 — Epsilon subunit of F1F0-ATP synthase N-terminal domain
Superfamily Superfamily superfamilyb.93.1 — Epsilon subunit of F1F0-ATP synthase N-terminal domain
Family Family familyb.93.1.1 — Epsilon subunit of F1F0-ATP synthase N-terminal domain

CATH v4.4 (2 domains)

Domain ID domain_id1aqtA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology15 — ATP Synthase; domain 1
Homologous superfamily homologous superfamily10 — F0F1 ATP synthase delta/epsilon subunit, N-terminal
Domain ID domain_id1aqtA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily440 — ATP synthase delta/epsilon subunit, C-terminal domain
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8. Citations (2)

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9. Files and Curves (10)