8cs9

Composite reconstruction of Class 1 of the erythrocyte ankyrin-1 complex

Method: ELECTRON MICROSCOPY Dmax: 283.0 Å Quality: GOOD

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

Ankyrin-1

OrganismNot specified

UniProt P16157

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 Heteromer Protein × 18 其他Polymer 3 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 1–1881 Not recorded Blood group Rh(CE) polypeptide × 1 (P18577) Ammonium transporter Rh type A × 2 (Q02094) Protein 4.2 × 1 (P16452) Glycophorin-B × 1 (P06028) Glycophorin-A × 6 (P02724) Band 3 anion transport protein × 6 (P02730) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CLR CHOLESTEROL × 8 AJP Digitonin × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 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 × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification. cryo-EM vitrification conditions:Cryogen ETHANE;4-6 seconds, wait time 30 seconds Resolution 2.74 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.

20 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANK1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1881; UniProt 1–1881

Blood group Rh(CE) polypeptide

OrganismNot specified

UniProt P18577

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 Heteromer Protein × 18 其他Polymer 3 PDB declaration: octadecameric(18) Consistent with protein copy count Chain K; UniProt 1–417 Not recorded Ankyrin-1 × 1 (P16157) Ammonium transporter Rh type A × 2 (Q02094) Protein 4.2 × 1 (P16452) Glycophorin-B × 1 (P06028) Glycophorin-A × 6 (P02724) Band 3 anion transport protein × 6 (P02730) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CLR CHOLESTEROL × 8 AJP Digitonin × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 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 × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification. cryo-EM vitrification conditions:Cryogen ETHANE;4-6 seconds, wait time 30 seconds Resolution 2.74 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RHCE_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain K; PDBConstruct 1–417; UniProt 1–417

Ammonium transporter Rh type A

OrganismNot specified

UniProt Q02094

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 Heteromer Protein × 18 其他Polymer 3 PDB declaration: octadecameric(18) Consistent with protein copy count Chain L; UniProt 1–409 Chain Q; UniProt 1–409 Not recorded Ankyrin-1 × 1 (P16157) Blood group Rh(CE) polypeptide × 1 (P18577) Protein 4.2 × 1 (P16452) Glycophorin-B × 1 (P06028) Glycophorin-A × 6 (P02724) Band 3 anion transport protein × 6 (P02730) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CLR CHOLESTEROL × 8 AJP Digitonin × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 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 × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification. cryo-EM vitrification conditions:Cryogen ETHANE;4-6 seconds, wait time 30 seconds Resolution 2.74 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RHAG_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain L; PDBConstruct 1–409; UniProt 1–409 Author chain Q; PDBConstruct 1–409; UniProt 1–409

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 Other combination Heteromer Protein × 18 其他Polymer 3 PDB declaration: octadecameric(18) Consistent with protein copy count Chain X; UniProt 1–691 Not recorded Ankyrin-1 × 1 (P16157) Blood group Rh(CE) polypeptide × 1 (P18577) Ammonium transporter Rh type A × 2 (Q02094) Glycophorin-B × 1 (P06028) Glycophorin-A × 6 (P02724) Band 3 anion transport protein × 6 (P02730) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CLR CHOLESTEROL × 8 AJP Digitonin × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 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 × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification. cryo-EM vitrification conditions:Cryogen ETHANE;4-6 seconds, wait time 30 seconds Resolution 2.74 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 4
Chains and sequence ranges Author chain X; PDBConstruct 1–691; UniProt 1–691

Glycophorin-B

OrganismNot specified

UniProt P06028

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 Heteromer Protein × 18 其他Polymer 3 PDB declaration: octadecameric(18) Consistent with protein copy count Chain P; UniProt 1–91 Not recorded Ankyrin-1 × 1 (P16157) Blood group Rh(CE) polypeptide × 1 (P18577) Ammonium transporter Rh type A × 2 (Q02094) Protein 4.2 × 1 (P16452) Glycophorin-A × 6 (P02724) Band 3 anion transport protein × 6 (P02730) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CLR CHOLESTEROL × 8 AJP Digitonin × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 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 × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification. cryo-EM vitrification conditions:Cryogen ETHANE;4-6 seconds, wait time 30 seconds Resolution 2.74 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLPB_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain P; PDBConstruct 1–91; UniProt 1–91

Glycophorin-A

OrganismNot specified

UniProt P02724

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 Heteromer Protein × 18 其他Polymer 3 PDB declaration: octadecameric(18) Consistent with protein copy count Chain R; UniProt 1–150 Chain S; UniProt 1–150 Chain T; UniProt 1–150 Chain a; UniProt 1–150 Chain b; UniProt 1–150 Chain c; UniProt 1–150 Not recorded Ankyrin-1 × 1 (P16157) Blood group Rh(CE) polypeptide × 1 (P18577) Ammonium transporter Rh type A × 2 (Q02094) Protein 4.2 × 1 (P16452) Glycophorin-B × 1 (P06028) Band 3 anion transport protein × 6 (P02730) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CLR CHOLESTEROL × 8 AJP Digitonin × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 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 × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification. cryo-EM vitrification conditions:Cryogen ETHANE;4-6 seconds, wait time 30 seconds Resolution 2.74 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.

15 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLPA_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain R; PDBConstruct 1–150; UniProt 1–150 Author chain S; PDBConstruct 1–150; UniProt 1–150 Author chain T; PDBConstruct 1–150; UniProt 1–150 Author chain a; PDBConstruct 1–150; UniProt 1–150 Author chain b; PDBConstruct 1–150; UniProt 1–150 Author chain c; PDBConstruct 1–150; UniProt 1–150

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 Heteromer Protein × 18 其他Polymer 3 PDB declaration: octadecameric(18) Consistent with protein copy count Chain V; UniProt 1–911 Chain Y; UniProt 1–911 Chain Z; UniProt 1–911 Chain e; UniProt 1–911 Chain f; UniProt 1–911 Chain g; UniProt 1–911 Not recorded Ankyrin-1 × 1 (P16157) Blood group Rh(CE) polypeptide × 1 (P18577) Ammonium transporter Rh type A × 2 (Q02094) Protein 4.2 × 1 (P16452) Glycophorin-B × 1 (P06028) Glycophorin-A × 6 (P02724) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CLR CHOLESTEROL × 8 AJP Digitonin × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 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 × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification. cryo-EM vitrification conditions:Cryogen ETHANE;4-6 seconds, wait time 30 seconds Resolution 2.74 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 7
Chains and sequence ranges Author chain V; PDBConstruct 1–911; UniProt 1–911 Author chain Y; PDBConstruct 1–911; UniProt 1–911 Author chain Z; PDBConstruct 1–911; UniProt 1–911 Author chain e; PDBConstruct 1–911; UniProt 1–911 Author chain f; PDBConstruct 1–911; UniProt 1–911 Author chain g; 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 8cs9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8cs9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8cs9
Deposition date deposition_date2022-05-12
Structure title titleComposite reconstruction of Class 1 of the erythrocyte ankyrin-1 complex
Keywords keywordsMembrane Protein, Anion Exchange, Erythrocyte, Glycoprotein, TRANSPORT PROTEIN-STRUCTURAL PROTEIN complex; TRANSPORT PROTEIN/STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier82.65
Radius of gyration Rg (electron density) rg_electron82.72
Forward intensity I(0) i08716850000.00
Molecular weight molecular_weight859890.0 kDa
Excluded volume excluded_volume1102800 ų
Envelope volume envelope_volume1875200 ų
Hydration-shell volume shell_volume189940 ų
Envelope diameter envelope_diameter271.0
Shell Rg shell_rg84.09
Envelope Rg envelope_rg78.16
Shape Rg shape_rg82.74
Total Rg total_rg82.65
Total atoms total_atoms60652
Residues n_residues7677
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 dmax283.0
Rg (real space) rg_real85.93
Rg uncertainty (real space) rg_real_error1.54
I(0) (real space) i0_real8.7170e+09
I(0) uncertainty (real space) i0_real_error1.8630e+08
Rg (reciprocal space) rg_reciprocal82.75
I(0) (reciprocal space) i0_reciprocal8719000000.0000
Solution quality estimate total_estimate0.8786
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary104.3
Skewness Skewness skewness0.417
Kurtosis Kurtosis kurtosis-0.099
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha1.1840
Highest regularization parameter α highest_alpha253600000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.859; Stabil: 0.879; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.239

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

8. Citations (1)

9. Files and Curves (10)