9w66

Cryo-EM structure of ATP bound state human ABCD3 in outward-facing conformation

Method: ELECTRON MICROSCOPY Dmax: 124.3 Å Quality: GOOD

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

ATP-binding cassette sub-family D member 3,Green fluorescent protein

Homo sapiens

UniProt P28288

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 Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–659 Mutation:E596Q ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 CLR CHOLESTEROL × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ABCD3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–659; UniProt 1–659

ATP-binding cassette sub-family D member 3,Green fluorescent protein

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 Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–238 Mutation:E596Q ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 CLR CHOLESTEROL × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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 669–906; UniProt 1–238

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 9w66

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9w66
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9w66
Deposition date deposition_date2025-08-03
Structure title titleCryo-EM structure of ATP bound state human ABCD3 in outward-facing conformation
Keywords keywordsABC transporter, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.28
Radius of gyration Rg (electron density) rg_electron35.34
Forward intensity I(0) i067813000.00
Molecular weight molecular_weight69045.0 kDa
Excluded volume excluded_volume88126 ų
Envelope volume envelope_volume120610 ų
Hydration-shell volume shell_volume31158 ų
Envelope diameter envelope_diameter131.5
Shell Rg shell_rg37.63
Envelope Rg envelope_rg35.44
Shape Rg shape_rg35.35
Total Rg total_rg35.48
Total atoms total_atoms4861
Residues n_residues581
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 dmax124.3
Rg (real space) rg_real35.72
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real6.7810e+07
I(0) uncertainty (real space) i0_real_error1.3500e+06
Rg (reciprocal space) rg_reciprocal35.45
I(0) (reciprocal space) i0_reciprocal67800000.0000
Solution quality estimate total_estimate0.8037
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.1
Skewness Skewness skewness0.607
Kurtosis Kurtosis kurtosis-0.276
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4859000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.673; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.668; Smooth: 0.757

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)