1bnx

STRUCTURAL STUDIES ON THE EFFECTS OF THE DELETION IN THE RED CELL ANION EXCHANGER (BAND3, AE1) ASSOCIATED WITH SOUTH EAST ASIAN OVALOCYTOSIS.

Method: SOLUTION NMR D_max: 60.4 Å Quality: REASONABLE

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

PROTEIN (BAND 3)

OrganismNot specified

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 388–429	Fragment：C-TERMINAL CYTOPLASM/FIRST MEMBRANE SPAN Mutation：A400-A408 DELETION Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 3.5；298 K；Pressure 1	Resolution not provided

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.

Other PDB	Difference from Current Entry 1BNX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BH7 A LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1998-06-16	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 803–835（33 aa） Fragment：FINAL CYTOPLASMIC LOOP	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；298 K；Ionic strength (raw mmCIF value) 12mM；Pressure ATMOSPHERIC NMR sample composition 30% TFE-D3/H2O	Resolution not provided
1BTQ THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3 Deposited 1994-08-03	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 405–424（20 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1BTR THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3 Deposited 1993-05-25	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 405–424（20 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1BTS THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3 Deposited 1994-08-03	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 436–456（21 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1BTT THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3 Deposited 1994-08-03	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 436–456（21 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1BZK STRUCTURAL STUDIES ON THE EFFECTS OF THE DELETION IN THE RED CELL ANION EXCHANGER (BAND3, AE1) ASSOCIATED WITH SOUTH EAST ASIAN OVALOCYTOSIS. Deposited 1998-11-01	Different construct Different mutation/modification	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 389–430（42 aa） Fragment：C-TERMINAL CYTOPLASM/FIRST MEMBRANE SPAN	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；298 K；Pressure 1	Resolution not provided
1HYN CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF HUMAN ERYTHROCYTE BAND-3 PROTEIN Deposited 2001-01-20	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain P 1–379（379 aa） Chain Q 1–379（379 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.8；METHOD: SITTING DROP VAPOR DIFFUSION WITH SEEDING. TEMPERATURE: 293 K. RESERVOIR: 50-53% SATURATED AMMONIUM SULFATE, 150mM SODIUM CITRATE PH 4.8. PROTEIN: 7 mg/ml PROTEIN IN 5mM SODIUM PHOSPHATE PH 6.8, 10 mM SODIUM CHLORIDE.	Resolution 2.60 Å R-free 0.290
1HYN CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF HUMAN ERYTHROCYTE BAND-3 PROTEIN Deposited 2001-01-20	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain R 1–379（379 aa） Chain S 1–379（379 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.8；METHOD: SITTING DROP VAPOR DIFFUSION WITH SEEDING. TEMPERATURE: 293 K. RESERVOIR: 50-53% SATURATED AMMONIUM SULFATE, 150mM SODIUM CITRATE PH 4.8. PROTEIN: 7 mg/ml PROTEIN IN 5mM SODIUM PHOSPHATE PH 6.8, 10 mM SODIUM CHLORIDE.	Resolution 2.60 Å R-free 0.290
1HYN CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF HUMAN ERYTHROCYTE BAND-3 PROTEIN Deposited 2001-01-20	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain P 1–379（379 aa） Chain Q 1–379（379 aa） Chain R 1–379（379 aa） Chain S 1–379（379 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.8；METHOD: SITTING DROP VAPOR DIFFUSION WITH SEEDING. TEMPERATURE: 293 K. RESERVOIR: 50-53% SATURATED AMMONIUM SULFATE, 150mM SODIUM CITRATE PH 4.8. PROTEIN: 7 mg/ml PROTEIN IN 5mM SODIUM PHOSPHATE PH 6.8, 10 mM SODIUM CHLORIDE.	Resolution 2.60 Å R-free 0.290
2BTA NMR STUDY OF N-TERMINAL HUMAN BAND 3 PEPTIDE, RESIDUES 1-15 Deposited 1995-11-13	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–15（15 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
2BTB NMR STUDY OF N-TERMINAL HUMAN BAND 3 PEPTIDE, RESIDUES 1-15 Deposited 1995-11-13	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–15（15 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
3BTB NMR SOLUTION STRUCTURE OF A BAND 3 PEPTIDE INHIBITOR BOUND TO GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, 20 STRUCTURES Deposited 1997-09-07	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–15（15 aa） Fragment：GLYCOLYTIC ENZYME-BINDING DOMAIN, N-TERMINAL 15 RESIDUES OF BAND 3 PROTEIN	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.5；283 K	Resolution not provided
4KY9 Structural and Functional Analysis of a Putative Substrate Access Tunnel in the Cytosolic Domain of Human Anion Exchanger 1 Deposited 2013-05-28	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 51–356（306 aa） Fragment：UNP residues 51-356 Chain P 51–356（306 aa） Fragment：UNP residues 51-356	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；100 mM BisTris pH 6.5, 18% PEG 3350, with 0.5% (w/v) octylglucoside, vapor diffusion, sitting drop, temperature 298K	Resolution 2.23 Å R-free 0.223
4YZF Crystal structure of the anion exchanger domain of human erythrocyte Band 3 Deposited 2015-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	4KU 2,2'-ethane-1,2-diylbis{5-[(sulfanylmethyl)amino]benzenesulfonic acid} × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；277 K；100 mM Tris-HCl (pH 8.0), 22-26 %(v/v) PEG300, 250 mM CH3COOK	Resolution 3.50 Å R-free 0.290
4YZF Crystal structure of the anion exchanger domain of human erythrocyte Band 3 Deposited 2015-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 1–911（911 aa） Chain D 1–911（911 aa）	Not recorded	4KU 2,2'-ethane-1,2-diylbis{5-[(sulfanylmethyl)amino]benzenesulfonic acid} × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；277 K；100 mM Tris-HCl (pH 8.0), 22-26 %(v/v) PEG300, 250 mM CH3COOK	Resolution 3.50 Å R-free 0.290
7TVZ Cryo-EM structure of human band 3-protein 4.2 complex in diagonal conformation Deposited 2022-02-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 LMT DODECYL-BETA-D-MALTOSIDE × 5 CLR CHOLESTEROL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
7TW0 Cryo-EM structure of human band 3-protein 4.2 complex in vertical conformation Deposited 2022-02-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	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
7TW1 Cryo-EM structure of human band 3-protein 4.2 complex (B2P2vertical) Deposited 2022-02-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.60 Å
7TW2 Cryo-EM structure of human band 3 dimer from red blood cell Deposited 2022-02-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.80 Å
7TW3 Cryo-EM structure of human ankyrin complex (B2P1A1) from red blood cell Deposited 2022-02-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.40 Å
7TW5 Cryo-EM structure of human ankyrin complex (B2P1A2) from red blood cell Deposited 2022-02-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.70 Å
7TW6 Cryo-EM structure of human ankyrin complex (B4P1A1) from red blood cell Deposited 2022-02-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–911（911 aa） Chain B 1–911（911 aa） Chain J 1–911（911 aa） Chain K 1–911（911 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.60 Å
7TY4 Cryo-EM structure of human Anion Exchanger 1 Deposited 2022-02-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	CLR CHOLESTEROL × 2 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 Y01 CHOLESTEROL HEMISUCCINATE × 6	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 2.99 Å
7TY6 Cryo-EM structure of human Anion Exchanger 1 bound to 4,4'-Diisothiocyanatodihydrostilbene-2,2'-Disulfonic Acid (H2DIDS) Deposited 2022-02-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	CLR CHOLESTEROL × 8 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 4DS 4,4'-Diisothiocyano-2,2'-stilbenedisulfonic acid × 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 2.98 Å
7TY7 Cryo-EM structure of human Anion Exchanger 1 bound to Bicarbonate Deposited 2022-02-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	BCT BICARBONATE ION × 2 CLR CHOLESTEROL × 7 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 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 3.37 Å
7TY8 Cryo-EM structure of human Anion Exchanger 1 bound to Niflumic Acid Deposited 2022-02-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	CLR CHOLESTEROL × 8 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 NFL 2-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}NICOTINIC ACID × 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 3.18 Å
7TYA Cryo-EM structure of human Anion Exchanger 1 modified with Diethyl Pyrocarbonate (DEPC) Deposited 2022-02-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CLR CHOLESTEROL × 8 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 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 3.07 Å
7UZ3 Band 3-Glycophorin A complex, outward facing Deposited 2022-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–911（911 aa） Chain E 1–911（911 aa）	Not recorded	CLR CHOLESTEROL × 4 PLC DIUNDECYL PHOSPHATIDYL CHOLINE × 2 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	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 2.35 Å
7UZU Ankyrin-1 (N-terminal region of membrane binding domain, local refinement from consensus reconstruction; bound to N-terminal peptide from band 3) Deposited 2022-05-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain W 1–911（911 aa）	Not recorded	No recorded non-water small molecule	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 2.30 Å
7UZV Cytoplasmic domains of Band 3-I (local refinement from consensus reconstruction of ankyrin complexes) Deposited 2022-05-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–911（911 aa） Chain E 1–911（911 aa）	Not recorded	No recorded non-water small molecule	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 2.50 Å
7V07 Band 3-I-TM local refinement from erythrocyte ankyrin-1 complex consensus reconstruction Deposited 2022-05-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–911（911 aa） Chain E 1–911（911 aa）	Not recorded	CLR CHOLESTEROL × 4 PLC DIUNDECYL PHOSPHATIDYL CHOLINE × 2 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	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 2.80 Å
7V0K Consensus refinement of human erythrocyte ankyrin-1 complex (Composite map) Deposited 2022-05-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain O 1–911（911 aa） Chain P 1–911（911 aa） Chain W 1–911（911 aa）	Not recorded	CLR CHOLESTEROL × 6 AJP Digitonin × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PLC DIUNDECYL PHOSPHATIDYL CHOLINE × 2 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	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 2.40 Å
7V0M Local refinement of ankyrin-1 (N-terminal half), class 1 of erythrocyte ankyrin-1 complex Deposited 2022-05-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain W 1–911（911 aa）	Not recorded	No recorded non-water small molecule	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 2.70 Å
7V0T Local refinement of Band 3-I cytoplasmic domains, class 1 of erythrocyte ankyrin-1 complex Deposited 2022-05-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–911（911 aa） Chain E 1–911（911 aa）	Not recorded	No recorded non-water small molecule	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
7V0U Local refinement of Band 3-II cytoplasmic domains, class 1 of erythrocyte ankyrin-1 complex Deposited 2022-05-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain D 1–911（911 aa） Chain F 1–911（911 aa）	Not recorded	No recorded non-water small molecule	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 3.00 Å
7V0Y Local refinement of Band 3-III cytoplasmic domains, class 1 of erythrocyte ankyrin-1 complex Deposited 2022-05-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–911（911 aa） Chain E 1–911（911 aa）	Not recorded	No recorded non-water small molecule	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 3.00 Å
7V19 Local refinement of Band 3-II transmembrane domains, class 1 of erythrocyte ankyrin-1 complex Deposited 2022-05-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–911（911 aa） Chain E 1–911（911 aa）	Not recorded	CLR CHOLESTEROL × 2 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	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 3.30 Å
8CRQ Local refinement of Band 3-I transmembrane domains, class 1 of erythrocyte ankyrin-1 complex Deposited 2022-05-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–911（911 aa） Chain E 1–911（911 aa）	Not recorded	CLR CHOLESTEROL × 2 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	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 3.20 Å
8CRR Local refinement of Band 3-III transmembrane domains, class 1 of erythrocyte ankyrin-1 complex Deposited 2022-05-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–911（911 aa） Chain E 1–911（911 aa）	Not recorded	CLR CHOLESTEROL × 2 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	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 3.00 Å
8CRT Local refinement of Rh trimer, glycophorin B and Band3-III transmembrane region, class 1a of erythrocyte ankyrin-1 complex Deposited 2022-05-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain C 1–911（911 aa） Chain E 1–911（911 aa）	Not recorded	CLR CHOLESTEROL × 2	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 3.00 Å
8CS9 Composite reconstruction of Class 1 of the erythrocyte ankyrin-1 complex Deposited 2022-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 18 PDB declaration: octadecameric	Chain V 1–911（911 aa） Chain Y 1–911（911 aa） Chain Z 1–911（911 aa） Chain e 1–911（911 aa） Chain f 1–911（911 aa） Chain g 1–911（911 aa）	Not recorded	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
8CSL Sub-tomogram averaging of erythrocyte ankyrin-1 complex Deposited 2022-05-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 19 PDB declaration: nonadecameric	Chain V 1–911（911 aa） Chain W 1–911（911 aa） Chain Y 1–911（911 aa） Chain Z 1–911（911 aa） Chain e 1–911（911 aa） Chain f 1–911（911 aa） Chain g 1–911（911 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；130 mM KCl, 10 mM HEPES, pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 25.00 Å
8CSV Local refinement of Anykyrin-1 (N-terminal half of membrane binding domain) in Class 2 of erythrocyte ankyrin-1 complex Deposited 2022-05-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain W 1–911（911 aa）	Not recorded	No recorded non-water small molecule	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 2.70 Å
8CSY Local refinement of cytoplasmic domains of band3-I in class 2 of erythrocyte ankyrin-1 complex Deposited 2022-05-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–911（911 aa） Chain E 1–911（911 aa）	Not recorded	No recorded non-water small molecule	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 2.70 Å
8CT3 Local refinement of band3-I transmembrane region from class 2 of erythrocyte ankyrin-1 complex Deposited 2022-05-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–911（911 aa） Chain E 1–911（911 aa）	Not recorded	CLR CHOLESTEROL × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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	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 3.30 Å
8CTE Class 2 of erythrocyte ankyrin-1 complex (Composite map) Deposited 2022-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain P 1–911（911 aa） Chain T 1–911（911 aa） Chain W 1–911（911 aa）	Not recorded	CLR CHOLESTEROL × 10 AJP Digitonin × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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	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 2.90 Å
8T3R Cryo-EM Analysis of AE1 Structure in 100 mM NaCl Buffer: Form1 Deposited 2023-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.99 Å
8T3U Cryo-EM Analysis of AE1 Structure in 100 mM NaCl Buffer: Form2 Deposited 2023-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PLC DIUNDECYL PHOSPHATIDYL CHOLINE × 2 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	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.97 Å
8T44 Cryo-EM Analysis of AE1 Structure in 100 mM NaHCO3 Buffer: Form1 Deposited 2023-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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 × 3 CO3 CARBONATE ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.12 Å
8T45 Cryo-EM Analysis of AE1 Structure in 100 mM NaHCO3 Buffer: Form2 Deposited 2023-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	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 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PLC DIUNDECYL PHOSPHATIDYL CHOLINE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.99 Å
8T47 Cryo-EM Analysis of AE1 Structure in 100 mM NaHCO3 Buffer: Form3 Deposited 2023-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain B 1–911（911 aa）	Not recorded	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 × 4 CO3 CARBONATE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.16 Å
8T6U Cryo-EM structure of human Anion Exchanger 1 bound to Dipyridamole Deposited 2023-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 369–891（523 aa） Chain B 369–891（523 aa）	Not recorded	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
8T6V Cryo-EM structure of human Anion Exchanger 1 bound to 4,4'-Diisothiocyanatostilbene-2,2'-Disulfonic Acid (DIDS) Deposited 2023-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 369–891（523 aa） Chain B 369–891（523 aa）	Not recorded	4DS 4,4'-Diisothiocyano-2,2'-stilbenedisulfonic acid × 2 CLR CHOLESTEROL × 6 Y01 CHOLESTEROL HEMISUCCINATE × 2 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 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 2.95 Å
9MND Band 3 OF/IF1 Deposited 2024-12-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain C 1–911（911 aa）	Not recorded	PLC DIUNDECYL PHOSPHATIDYL CHOLINE × 4 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	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.40 Å
9MNG Band 3 OF/OF Deposited 2024-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–911（911 aa） Chain C 1–911（911 aa）	Not recorded	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 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.11 Å
9MOS Band 3 IF1/IF2 Deposited 2024-12-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–911（911 aa） Chain C 1–911（911 aa）	Not recorded	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

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 2–34； UniProt 388–429

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1bnx
Deposition date deposition_date	1998-07-30
Structure title title	STRUCTURAL STUDIES ON THE EFFECTS OF THE DELETION IN THE RED CELL ANION EXCHANGER (BAND3, AE1) ASSOCIATED WITH SOUTH EAST ASIAN OVALOCYTOSIS.
Keywords keywords	HUMAN ERYTHROCYTE ANION TRANSPORTER, TRANSMEMBRANE, SYNTHETIC PEPTIDE, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	16.05 Å
Radius of gyration Rg (electron density) rg_electron	15.35 Å
Forward intensity I(0) i0	68778700.00
Molecular weight molecular_weight	78904.0 kDa
Excluded volume excluded_volume	103180 Å³
Envelope volume envelope_volume	51775 Å³
Hydration-shell volume shell_volume	21891 Å³
Envelope diameter envelope_diameter	68.4 Å
Shell Rg shell_rg	26.23 Å
Envelope Rg envelope_rg	19.66 Å
Shape Rg shape_rg	15.30 Å
Total Rg total_rg	16.50 Å
Total atoms total_atoms	11193
Residues n_residues	693
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	60.4 Å
Rg (real space) rg_real	16.15 Å
Rg uncertainty (real space) rg_real_error	0.59 Å
I(0) (real space) i0_real	6.8780e+07
I(0) uncertainty (real space) i0_real_error	8.7460e+05
Rg (reciprocal space) rg_reciprocal	16.14 Å
I(0) (reciprocal space) i0_reciprocal	68780000.0000
Solution quality estimate total_estimate	0.7380
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	18.3 Å
Skewness Skewness skewness	0.452
Kurtosis Kurtosis kurtosis	-0.084
Angular range angular_range	— – 0.4950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	158900.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.648; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.650; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1bnxa_
Class class	j — Peptides
Fold Fold fold	j.35 — Transmembrane helical fragments
Superfamily Superfamily superfamily	j.35.1 — Transmembrane helical fragments
Family Family family	j.35.1.1 — Transmembrane helical fragments

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	PROTEIN (BAND 3)
Molecular weight formula_weight	3743.3 kDa
Mutation mutation	A400-A408 DELETION
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	11193

fit	/app/data/saxs_computation/bn/1bnx/1bnx.fit
pddf	/app/data/pr_computation/bn/1bnx/1bnx.pr.out
profile	/app/data/saxs_computation/bn/1bnx/1bnx.dat

STRUCTURAL STUDIES ON THE EFFECTS OF THE DELETION IN THE RED CELL ANION EXCHANGER (BAND3, AE1) ASSOCIATED WITH SOUTH EAST ASIAN OVALOCYTOSIS.

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

PROTEIN (BAND 3)

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)