SAXSdb — 4csk

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

AQUAPORIN-1

HOMO SAPIENS

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	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 9；pH 9	Resolution 3.28 Å R-free 0.298

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 4CSK	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 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 oligomeric state 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 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
6POJ STRUCTURAL REFINEMENT OF AQUAPORIN 1 VIA SSNMR Deposited 2019-07-04	Different oligomeric state 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
7UZE Erythrocyte ankyrin-1 complex class 2 local refinement of AQP1 (C4 symmetry applied) Deposited 2022-05-09	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） 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	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） 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 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 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 method 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 method 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 24–292； 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	4csk
Deposition date deposition_date	2014-03-08
Structure title title	human Aquaporin
Keywords keywords	TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	19.13 Å
Radius of gyration Rg (electron density) rg_electron	18.05 Å
Forward intensity I(0) i0	9762430.00
Molecular weight molecular_weight	24389.0 kDa
Excluded volume excluded_volume	31166 Å³
Envelope volume envelope_volume	36702 Å³
Hydration-shell volume shell_volume	17320 Å³
Envelope diameter envelope_diameter	70.2 Å
Shell Rg shell_rg	24.24 Å
Envelope Rg envelope_rg	18.76 Å
Shape Rg shape_rg	18.05 Å
Total Rg total_rg	19.13 Å
Total atoms total_atoms	1722
Residues n_residues	233
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	70.4 Å
Rg (real space) rg_real	19.17 Å
Rg uncertainty (real space) rg_real_error	0.57 Å
I(0) (real space) i0_real	9.7620e+06
I(0) uncertainty (real space) i0_real_error	1.2610e+05
Rg (reciprocal space) rg_reciprocal	19.17 Å
I(0) (reciprocal space) i0_reciprocal	9762000.0000
Solution quality estimate total_estimate	0.8257
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	22.5 Å
Skewness Skewness skewness	0.474
Kurtosis Kurtosis kurtosis	0.023
Angular range angular_range	— – 0.4150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2044000.0000
Real-space data points n_real_points	73
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.622; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.874; Smooth: 0.991

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	4cskA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1080 — Glycerol uptake facilitator protein
Homologous superfamily homologous superfamily	10 — Glycerol uptake facilitator protein.

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8. Citations (1)

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Unit-cell length a length_a	89.280 Å
Unit-cell length b length_b	89.280 Å
Unit-cell length c length_c	174.850 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	16

Space group space_group	I 4 2 2
Space-group number int_tables_number	97
Crystal system crystal_system	—

Resolution resolution	3.280 Å
Low-resolution limit resolution_low	12.490 Å
R factor r_factor	0.2368
R_work r_work	0.2338
R_free r_free	0.2978

Description description	AQUAPORIN-1
Molecular weight formula_weight	31165.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1728

human Aquaporin

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

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	SPODOPTERA FRUGIPERDA

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	6

fit	/app/data/saxs_computation/cs/4csk/4csk.fit
pddf	/app/data/pr_computation/cs/4csk/4csk.pr.out
profile	/app/data/saxs_computation/cs/4csk/4csk.dat