SAXSdb — 7uze

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

Aquaporin-1

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–269 Chain B； UniProt 1–269 Chain C； UniProt 1–269 Chain D； UniProt 1–269	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

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 7UZE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1FQY STRUCTURE OF AQUAPORIN-1 AT 3.8 A RESOLUTION BY ELECTRON CRYSTALLOGRAPHY Deposited 2000-09-07	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	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	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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
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	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	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	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	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	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	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

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	AQP1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–269； UniProt 1–269 Author chain B； PDBConstruct 1–269； UniProt 1–269 Author chain C； PDBConstruct 1–269； UniProt 1–269 Author chain D； PDBConstruct 1–269； UniProt 1–269

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	7uze
Deposition date deposition_date	2022-05-09
Structure title title	Erythrocyte ankyrin-1 complex class 2 local refinement of AQP1 (C4 symmetry applied)
Keywords keywords	Membrane Protein, Anion Exchange, Erythrocyte, Glycoprotein, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	28.10 Å
Radius of gyration Rg (electron density) rg_electron	27.34 Å
Forward intensity I(0) i0	148111000.00
Molecular weight molecular_weight	104960.0 kDa
Excluded volume excluded_volume	135210 Å³
Envelope volume envelope_volume	154380 Å³
Hydration-shell volume shell_volume	44224 Å³
Envelope diameter envelope_diameter	83.5 Å
Shell Rg shell_rg	36.84 Å
Envelope Rg envelope_rg	27.41 Å
Shape Rg shape_rg	27.37 Å
Total Rg total_rg	28.19 Å
Total atoms total_atoms	15076
Residues n_residues	984
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	83.6 Å
Rg (real space) rg_real	27.84 Å
Rg uncertainty (real space) rg_real_error	0.36 Å
I(0) (real space) i0_real	1.4810e+08
I(0) uncertainty (real space) i0_real_error	1.7930e+06
Rg (reciprocal space) rg_reciprocal	27.92 Å
I(0) (reciprocal space) i0_reciprocal	148100000.0000
Solution quality estimate total_estimate	0.9032
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	37.3 Å
Skewness Skewness skewness	0.042
Kurtosis Kurtosis kurtosis	-0.518
Angular range angular_range	— – 0.2800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	29830000.0000
Real-space data points n_real_points	57
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.975

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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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	—

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

Resolution resolution	2.40 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	108425

Description description	Aquaporin-1
Molecular weight formula_weight	28788.3 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,B,C,A
Atom count atom_count	15289

Erythrocyte ankyrin-1 complex class 2 local refinement of AQP1 (C4 symmetry applied)

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

Aquaporin-1

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	CHOLESTEROL
Molecular weight formula_weight	386.7 kDa
Source method src_method	syn
Copy count entity_count	4

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	113

fit	/app/data/saxs_computation/uz/7uze/7uze.fit
pddf	/app/data/pr_computation/uz/7uze/7uze.pr.out
profile	/app/data/saxs_computation/uz/7uze/7uze.dat