8xtw

Structure of human VAChT in complex with acetylcholine

Method: ELECTRON MICROSCOPY Dmax: 66.9 Å Quality: EXCELLENT

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

Vesicular acetylcholine transporter,Green fluorescent protein,antibody

Homo sapiens

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–229 Mutation:S30R,Y39N,F64L,S65T,Q80R,F99S,N105T,Y145F,M153T,V163A,I171V,A206V ACH ACETYLCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 27–254; UniProt 2–229

Vesicular acetylcholine transporter,Green fluorescent protein,antibody

Homo sapiens

UniProt Q16572

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–26 Chain A; UniProt 27–476 Mutation:S30R,Y39N,F64L,S65T,Q80R,F99S,N105T,Y145F,M153T,V163A,I171V,A206V ACH ACETYLCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VACHT_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–26; UniProt 1–26 Author chain A; PDBConstruct 255–704; UniProt 27–476

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 8xtw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8xtw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8xtw
Deposition date deposition_date2024-01-12
Structure title titleStructure of human VAChT in complex with acetylcholine
Keywords keywordsTransporter, Membrane protein, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier21.79
Radius of gyration Rg (electron density) rg_electron20.78
Forward intensity I(0) i022975000.00
Molecular weight molecular_weight40923.0 kDa
Excluded volume excluded_volume53140 ų
Envelope volume envelope_volume63373 ų
Hydration-shell volume shell_volume24845 ų
Envelope diameter envelope_diameter67.6
Shell Rg shell_rg27.99
Envelope Rg envelope_rg20.99
Shape Rg shape_rg20.79
Total Rg total_rg21.79
Total atoms total_atoms2886
Residues n_residues382
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 dmax66.9
Rg (real space) rg_real21.66
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real2.2980e+07
I(0) uncertainty (real space) i0_real_error2.5160e+05
Rg (reciprocal space) rg_reciprocal21.69
I(0) (reciprocal space) i0_reciprocal22980000.0000
Solution quality estimate total_estimate0.9067
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.187
Kurtosis Kurtosis kurtosis-0.441
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4721000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)