9x4a

Cryo-EM structure of Streptococcus thermophilus FoeAB E504Q mutant in complex with ATP

Method: ELECTRON MICROSCOPY Dmax: 124.6 Å Quality: GOOD

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

Lipid/multidrug/protein-type ABC exporter, ATP binding/membrane-spanning protein

Streptococcus thermophilus

UniProt Q5M4V8

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 1–579 Not recorded Lipid/multidrug/protein-type ABC exporter, ATP binding/membrane-spanning protein × 1 (Q5M4V7) ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 2 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.16 Å

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5M4V8_STRT2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–579; UniProt 1–579

Lipid/multidrug/protein-type ABC exporter, ATP binding/membrane-spanning protein

Streptococcus thermophilus

UniProt Q5M4V7

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 42–623 Mutation:E504Q Lipid/multidrug/protein-type ABC exporter, ATP binding/membrane-spanning protein × 1 (Q5M4V8) ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 2 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.16 Å

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5M4V7_STRT2
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–582; UniProt 42–623

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 9x4a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9x4a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9x4a
Deposition date deposition_date2025-10-10
Structure title titleCryo-EM structure of Streptococcus thermophilus FoeAB E504Q mutant in complex with ATP
Keywords keywordsTRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.96
Radius of gyration Rg (electron density) rg_electron37.56
Forward intensity I(0) i0233520000.00
Molecular weight molecular_weight129210.0 kDa
Excluded volume excluded_volume164200 ų
Envelope volume envelope_volume208240 ų
Hydration-shell volume shell_volume47919 ų
Envelope diameter envelope_diameter131.8
Shell Rg shell_rg41.90
Envelope Rg envelope_rg37.71
Shape Rg shape_rg37.54
Total Rg total_rg37.91
Total atoms total_atoms9087
Residues n_residues1140
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax124.6
Rg (real space) rg_real37.33
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real2.3350e+08
I(0) uncertainty (real space) i0_real_error4.2300e+06
Rg (reciprocal space) rg_reciprocal37.10
I(0) (reciprocal space) i0_reciprocal233500000.0000
Solution quality estimate total_estimate0.8067
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.8
Skewness Skewness skewness0.603
Kurtosis Kurtosis kurtosis-0.228
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha70940000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.710; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.828; Smooth: 0.525

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)