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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P29972 New Search
10PDB entries
10Biological assembly
25chain/assembly records
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
1FQY STRUCTURE OF AQUAPORIN-1 AT 3.8 A RESOLUTION BY ELECTRON CRYSTALLOGRAPHY Deposited 2000-09-07 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–269（269 aa）
Not recorded No recorded non-water small molecule ELECTRON CRYSTALLOGRAPHY
X-ray crystallization conditions Dialysis with continuous flow dialysis machine；pH 6；298 K；Escherichia coli lipids, magnesium chloride, sodium chloride, MES, pH 6.0, Dialysis with continuous flow dialysis machine, temperature 298K
Resolution 3.80 Å R-free 0.417
1H6I A REFINED STRUCTURE OF HUMAN AQUAPORIN 1 Deposited 2001-06-15 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–269（269 aa）
Not recorded No recorded non-water small molecule ELECTRON CRYSTALLOGRAPHY mmCIF provides none of the parsed conditions Resolution 3.54 Å R-free 0.376
1IH5 CRYSTAL STRUCTURE OF AQUAPORIN-1 Deposited 2001-04-18 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–269（269 aa）
Not recorded No recorded non-water small molecule ELECTRON CRYSTALLOGRAPHY mmCIF provides none of the parsed conditions Resolution 3.70 Å R-free 0.458
4CSK human Aquaporin Deposited 2014-03-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–269（269 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 9；pH 9
Resolution 3.28 Å R-free 0.298
6POJ STRUCTURAL REFINEMENT OF AQUAPORIN 1 VIA SSNMR Deposited 2019-07-04 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–269（269 aa）
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7；278 K；Ionic strength (raw mmCIF value) 10 mM NaCl；Pressure 1
NMR sample composition 2 w/v [U-13C; U-15N] AQUAPORIN 1, NMR buffer | NMR buffer
Resolution not provided
7UZE Erythrocyte ankyrin-1 complex class 2 local refinement of AQP1 (C4 symmetry applied) Deposited 2022-05-09 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–269（269 aa）
Chain B 1–269（269 aa）
Chain C 1–269（269 aa）
Chain D 1–269（269 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CLR CHOLESTEROL × 4 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 2.40 Å
8CT2 Local refinement of AQP1 tetramer (C1; refinement mask included D1 of protein 4.2 and Ankyrin-1 AR1-5) in Class 2 of erythrocyte ankyrin-1 complex Deposited 2022-05-13 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–269（269 aa）
Chain B 1–269（269 aa）
Chain C 1–269（269 aa）
Chain D 1–269（269 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CLR CHOLESTEROL × 4 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 3.10 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 M 1–269（269 aa）
Chain O 1–269（269 aa）
Chain R 1–269（269 aa）
Chain S 1–269（269 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) 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
9ZCZ C4 local refinement of stomatin-bound aquaporin (human) Deposited 2025-11-24 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 3–249（247 aa）
Chain B 3–249（247 aa）
Chain C 3–249（247 aa）
Chain D 3–249（247 aa）
Not recorded CLR CHOLESTEROL × 4 PLM PALMITIC ACID × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.30 Å
9ZD2 C1 local refinement of aquaporin 1 bound to endogenous human stomatin Deposited 2025-11-24 Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric（9） Consistent with protein count
Chain A 3–249（247 aa）
Chain B 3–249（247 aa）
Chain C 3–249（247 aa）
Chain D 3–249（247 aa）
Not recorded PLM PALMITIC ACID × 4 CLR CHOLESTEROL × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.