9xou

CryoEM structure of LacY with Trimbody

Method: ELECTRON MICROSCOPY Dmax: 156.4 Å Quality: GOOD

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

H3-PrAC-5350A,2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase

Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

UniProt Q9WXS1

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 2–205 Chain B; UniProt 2–205 Chain C; UniProt 2–205 Not recorded LacY-nanobody-TAIL × 3 Lactose permease × 3 (P02920) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.50 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.

16 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9WXS1_THEMA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 118–321; UniProt 2–205 Author chain B; PDBConstruct 118–321; UniProt 2–205 Author chain C; PDBConstruct 118–321; UniProt 2–205

Lactose permease

Escherichia coli K-12

UniProt P02920

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain G; UniProt 1–417 Chain H; UniProt 1–417 Chain I; UniProt 1–417 Not recorded H3-PrAC-5350A,2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase × 3 (Q9WXS1) LacY-nanobody-TAIL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.50 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.

13 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LACY_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–417; UniProt 1–417 Author chain H; PDBConstruct 1–417; UniProt 1–417 Author chain I; PDBConstruct 1–417; UniProt 1–417

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 9xou

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9xou
Deposition date deposition_date2025-11-15
Structure title titleCryoEM structure of LacY with Trimbody
Keywords keywordsSTRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier57.21
Radius of gyration Rg (electron density) rg_electron58.14
Forward intensity I(0) i01198320000.00
Molecular weight molecular_weight316670.0 kDa
Excluded volume excluded_volume406970 ų
Envelope volume envelope_volume599000 ų
Hydration-shell volume shell_volume88371 ų
Envelope diameter envelope_diameter167.9
Shell Rg shell_rg58.15
Envelope Rg envelope_rg56.03
Shape Rg shape_rg58.21
Total Rg total_rg57.84
Total atoms total_atoms22382
Residues n_residues2870
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 dmax156.4
Rg (real space) rg_real56.94
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real1.1980e+09
I(0) uncertainty (real space) i0_real_error1.8210e+07
Rg (reciprocal space) rg_reciprocal57.40
I(0) (reciprocal space) i0_reciprocal1199000000.0000
Solution quality estimate total_estimate0.8461
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary92.7
Skewness Skewness skewness-0.039
Kurtosis Kurtosis kurtosis-0.771
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44750000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.999; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)