9x47

Cryo-EM structure of nucleotide-free Streptococcus thermophilus FoeAB 1

Method: ELECTRON MICROSCOPY Dmax: 127.7 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) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.20 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 Not recorded Lipid/multidrug/protein-type ABC exporter, ATP binding/membrane-spanning protein × 1 (Q5M4V8) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.20 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 9x47

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9x47
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9x47
Deposition date deposition_date2025-10-10
Structure title titleCryo-EM structure of nucleotide-free Streptococcus thermophilus FoeAB 1
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_guinier38.11
Radius of gyration Rg (electron density) rg_electron38.23
Forward intensity I(0) i0226105000.00
Molecular weight molecular_weight128410.0 kDa
Excluded volume excluded_volume163680 ų
Envelope volume envelope_volume218250 ų
Hydration-shell volume shell_volume48884 ų
Envelope diameter envelope_diameter128.9
Shell Rg shell_rg43.45
Envelope Rg envelope_rg37.01
Shape Rg shape_rg38.22
Total Rg total_rg38.62
Total atoms total_atoms9041
Residues n_residues1142
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 dmax127.7
Rg (real space) rg_real38.22
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real2.2610e+08
I(0) uncertainty (real space) i0_real_error3.0660e+06
Rg (reciprocal space) rg_reciprocal38.16
I(0) (reciprocal space) i0_reciprocal226100000.0000
Solution quality estimate total_estimate0.8822
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.6
Skewness Skewness skewness0.387
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27920000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.879; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.850

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)