7v0t

Local refinement of Band 3-I cytoplasmic domains, class 1 of erythrocyte ankyrin-1 complex

Method: ELECTRON MICROSCOPY Dmax: 82.6 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 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–911 Chain E; UniProt 1–911 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Final gel filtration buffer contained 0.05 % (w/v) digitonin, 130mM KCl, 20mM HEPES pH 7.4, 1mM ATP, 1mM MgCl2, 1mM PMSF. Peak fractions were concentrated to 8mg/mL, and 0.01% (w/v) of glycyrrhizic acid was added immediately prior to vitrification. cryo-EM vitrification conditions:Cryogen ETHANE;4-6 seconds, wait time 30 seconds Resolution 2.70 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 C; PDBConstruct 1–911; UniProt 1–911 Author chain E; 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 7v0t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7v0t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7v0t
Deposition date deposition_date2022-05-11
Structure title titleLocal refinement of Band 3-I cytoplasmic domains, class 1 of erythrocyte ankyrin-1 complex
Keywords keywordsMembrane Protein, ankyrin complex, Erythrocyte, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier27.33
Radius of gyration Rg (electron density) rg_electron26.03
Forward intensity I(0) i068803400.00
Molecular weight molecular_weight65415.0 kDa
Excluded volume excluded_volume82309 ų
Envelope volume envelope_volume100520 ų
Hydration-shell volume shell_volume31783 ų
Envelope diameter envelope_diameter87.2
Shell Rg shell_rg33.99
Envelope Rg envelope_rg26.20
Shape Rg shape_rg26.02
Total Rg total_rg26.96
Total atoms total_atoms4619
Residues n_residues584
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 dmax82.6
Rg (real space) rg_real27.27
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real6.8800e+07
I(0) uncertainty (real space) i0_real_error8.6430e+05
Rg (reciprocal space) rg_reciprocal27.29
I(0) (reciprocal space) i0_reciprocal68800000.0000
Solution quality estimate total_estimate0.9081
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.274
Kurtosis Kurtosis kurtosis-0.551
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18090000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.961; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.918

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)