7tw0

Cryo-EM structure of human band 3-protein 4.2 complex in vertical conformation

Method: ELECTRON MICROSCOPY Dmax: 190.5 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–911 Chain B; UniProt 1–911 Not recorded Protein 4.2 × 1 (P16452) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.60 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 B; PDBConstruct 1–911; UniProt 1–911

Protein 4.2

OrganismNot specified

UniProt P16452

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–691 Not recorded Band 3 anion transport protein × 2 (P02730) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.60 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EPB42_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–691; UniProt 1–691

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 7tw0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7tw0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7tw0
Deposition date deposition_date2022-02-06
Structure title titleCryo-EM structure of human band 3-protein 4.2 complex in vertical conformation
Keywords keywordsRed blood cell, Ankyrin complex, membrane protein, band 3, protein 4.2; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.91
Radius of gyration Rg (electron density) rg_electron53.13
Forward intensity I(0) i0858371000.00
Molecular weight molecular_weight258810.0 kDa
Excluded volume excluded_volume330400 ų
Envelope volume envelope_volume492010 ų
Hydration-shell volume shell_volume80027 ų
Envelope diameter envelope_diameter207.1
Shell Rg shell_rg54.08
Envelope Rg envelope_rg51.55
Shape Rg shape_rg53.12
Total Rg total_rg53.21
Total atoms total_atoms18266
Residues n_residues2309
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 dmax190.5
Rg (real space) rg_real53.10
Rg uncertainty (real space) rg_real_error2.21
I(0) (real space) i0_real8.5840e+08
I(0) uncertainty (real space) i0_real_error1.7060e+07
Rg (reciprocal space) rg_reciprocal52.75
I(0) (reciprocal space) i0_reciprocal857900000.0000
Solution quality estimate total_estimate0.8568
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary63.5
Skewness Skewness skewness0.466
Kurtosis Kurtosis kurtosis-0.078
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76620000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.773; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.822

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)