Current Protein Identity:P02724 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1AFO DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES Deposited 1997-03-11 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 81–120(40 aa) Fragment:TRANSMEMBRANE PEPTIDE
Chain B 81–120(40 aa) Fragment:TRANSMEMBRANE PEPTIDE
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6;313 K
Resolution not provided
2KPE Refined structure of Glycophorin A transmembrane segment dimer in DPC micelles Deposited 2009-10-13 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 89–117(29 aa) Fragment:transmembrane segment (UNP residues 89-117)
Chain B 89–117(29 aa) Fragment:transmembrane segment (UNP residues 89-117)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.5;313 K;Ionic strength (raw mmCIF value) 0;Pressure ambient
NMR sample composition 3 mM [U-100% 13C; U-100% 15N] GpA, 3 mM GpA, 180 mM [U-2H] DPC, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
2KPF Spatial structure of the dimeric transmembrane domain of glycophorin A in bicelles soluton Deposited 2009-10-13 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 80–117(38 aa) Fragment:transmembrane domain (UNP residues 80-117)
Chain B 80–117(38 aa) Fragment:transmembrane domain (UNP residues 80-117)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.5;313 K;Ionic strength (raw mmCIF value) 0;Pressure ambient
NMR sample composition 1mM unlabeled Glycophorin A, 1mM 13-C/15-N labeled Glycophorin A, 16mM DMPC d-54, 64 mM DHPC d-22, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
5EH4 Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase Deposited 2015-10-28 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 89–117(29 aa) Fragment:unp residues 89-117
Chain B 89–117(29 aa) Fragment:unp residues 89-117
Mutation:M81I Non-standard monomer:Yes (specific site not provided by mmCIF) Mutation:M81I Non-standard monomer:Yes (specific site not provided by mmCIF) OLB (2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE;293 K;20% (w/v)PEG 8000, 0.1 M sodium HEPES pH 7.5 10 mM TRIS-HCl pH 8, 40 mM NaCl
Resolution 2.81 Å R-free 0.260
5EH4 Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase Deposited 2015-10-28 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain C 89–117(29 aa) Fragment:unp residues 89-117
Chain D 89–117(29 aa) Fragment:unp residues 89-117
Mutation:M81I Non-standard monomer:Yes (specific site not provided by mmCIF) Mutation:M81I Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE;293 K;20% (w/v)PEG 8000, 0.1 M sodium HEPES pH 7.5 10 mM TRIS-HCl pH 8, 40 mM NaCl
Resolution 2.81 Å R-free 0.260
5EH6 Crystal Structure of the Glycophorin A Transmembrane Monomer in Lipidic Cubic Phase Deposited 2015-10-28 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 89–117(29 aa) Fragment:unp resideus 89-117
Mutation:M100I Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE;pH 7.5;293 K;0.1 M HEPES, 20% PEG8000, 10 mM Tris, 40 mM NaCl
Resolution 1.92 Å R-free 0.238
7UZ3 Band 3-Glycophorin A complex, outward facing Deposited 2022-05-08 Assembly 1 Other combination Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain B 1–150(150 aa)
Chain D 1–150(150 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
7V07 Band 3-I-TM local refinement from erythrocyte ankyrin-1 complex consensus reconstruction Deposited 2022-05-10 Assembly 1 Other combination Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain B 1–150(150 aa)
Chain D 1–150(150 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 Assembly 1 Protein heterocomplex Heteromer;Protein × 10 PDB declaration: decameric(10) Consistent with protein count
Chain D 1–150(150 aa)
Chain N 1–150(150 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
7V19 Local refinement of Band 3-II transmembrane domains, class 1 of erythrocyte ankyrin-1 complex Deposited 2022-05-11 Assembly 1 Other combination Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain B 1–150(150 aa)
Chain D 1–150(150 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 Assembly 1 Other combination Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain B 1–150(150 aa)
Chain D 1–150(150 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 Assembly 1 Other combination Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain B 1–150(150 aa)
Chain D 1–150(150 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 Assembly 1 Other combination Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
Chain B 1–150(150 aa)
Chain D 1–150(150 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 Assembly 1 Other combination Heteromer;Protein × 18 PDB declaration: octadecameric(18) Consistent with protein count
Chain R 1–150(150 aa)
Chain S 1–150(150 aa)
Chain T 1–150(150 aa)
Chain a 1–150(150 aa)
Chain b 1–150(150 aa)
Chain c 1–150(150 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 Assembly 1 Protein heterocomplex Heteromer;Protein × 19 PDB declaration: nonadecameric(19) Consistent with protein count
Chain R 1–150(150 aa)
Chain S 1–150(150 aa)
Chain T 1–150(150 aa)
Chain a 1–150(150 aa)
Chain b 1–150(150 aa)
Chain c 1–150(150 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
8CT3 Local refinement of band3-I transmembrane region from class 2 of erythrocyte ankyrin-1 complex Deposited 2022-05-13 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain B 1–150(150 aa)
Chain D 1–150(150 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 Assembly 1 Protein heterocomplex Heteromer;Protein × 14 PDB declaration: tetradecameric(14) Consistent with protein count
Chain D 1–150(150 aa)
Chain N 1–150(150 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