9mos

Band 3 IF1/IF2

Method: ELECTRON MICROSCOPY Dmax: 111.8 Å Quality: EXCELLENT

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

Band 3 anion transport protein

OrganismNot specified

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 1–911 Chain C; UniProt 1–911 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 2 PLC DIUNDECYL PHOSPHATIDYL CHOLINE × 2 CL CHLORIDE ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.88 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 1–911; UniProt 1–911 Author chain C; PDBConstruct 1–911; UniProt 1–911

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 9mos

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9mos
Deposition date deposition_date2024-12-27
Structure title titleBand 3 IF1/IF2
Keywords keywordsmembrane protein, transorter, chloride, bicarbonate, pip2, red blood cell, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.50
Radius of gyration Rg (electron density) rg_electron33.95
Forward intensity I(0) i0147567000.00
Molecular weight molecular_weight111310.0 kDa
Excluded volume excluded_volume145330 ų
Envelope volume envelope_volume181660 ų
Hydration-shell volume shell_volume44670 ų
Envelope diameter envelope_diameter115.3
Shell Rg shell_rg40.57
Envelope Rg envelope_rg33.35
Shape Rg shape_rg33.97
Total Rg total_rg34.42
Total atoms total_atoms16058
Residues n_residues969
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 dmax111.8
Rg (real space) rg_real34.46
Rg uncertainty (real space) rg_real_error1.24
I(0) (real space) i0_real1.4760e+08
I(0) uncertainty (real space) i0_real_error2.3170e+06
Rg (reciprocal space) rg_reciprocal34.49
I(0) (reciprocal space) i0_reciprocal147600000.0000
Solution quality estimate total_estimate0.9021
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.9
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.512
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15750000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)