8t6u

Cryo-EM structure of human Anion Exchanger 1 bound to Dipyridamole

Method: ELECTRON MICROSCOPY Dmax: 120.0 Å Quality: GOOD

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

Band 3 anion transport protein

Homo sapiens

UniProt P02730

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 369–891 Chain B; UniProt 369–891 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CLR CHOLESTEROL × 8 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 H9F 2-[[2-[bis(2-hydroxyethyl)amino]-4,8-di(piperidin-1-yl)pyrimido[5,4-d]pyrimidin-6-yl]-(2-hydroxyethyl)amino]ethanol × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force 3 for 3-5 seconds was used and subsequent grids were screened for ice thickness prior to data collection Resolution 3.13 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.

53 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B3AT_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–523; UniProt 369–891 Author chain B; PDBConstruct 1–523; UniProt 369–891

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 8t6u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t6u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t6u
Deposition date deposition_date2023-06-18
Structure title titleCryo-EM structure of human Anion Exchanger 1 bound to Dipyridamole
Keywords keywordsTransmembrane, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.72
Radius of gyration Rg (electron density) rg_electron35.33
Forward intensity I(0) i0162331000.00
Molecular weight molecular_weight121670.0 kDa
Excluded volume excluded_volume160450 ų
Envelope volume envelope_volume195240 ų
Hydration-shell volume shell_volume46734 ų
Envelope diameter envelope_diameter123.8
Shell Rg shell_rg41.09
Envelope Rg envelope_rg34.97
Shape Rg shape_rg35.36
Total Rg total_rg35.66
Total atoms total_atoms8602
Residues n_residues1032
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 dmax120.0
Rg (real space) rg_real35.80
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real1.6230e+08
I(0) uncertainty (real space) i0_real_error2.5600e+06
Rg (reciprocal space) rg_reciprocal35.75
I(0) (reciprocal space) i0_reciprocal162300000.0000
Solution quality estimate total_estimate0.8832
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.2
Skewness Skewness skewness0.369
Kurtosis Kurtosis kurtosis-0.439
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16680000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.872

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)