SAXSdb — 8amw

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

Aquaporin-7

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain A； UniProt 1–342 Chain B； UniProt 1–342 Chain C； UniProt 1–342 Chain D； UniProt 1–342 Chain E； UniProt 1–342 Chain F； UniProt 1–342 Chain G； UniProt 1–342 Chain H； UniProt 1–342	Not recorded	GOL GLYCEROL × 16	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE；3s blot, 3s wait, 0s drain time, 0 blot force	Resolution 3.00 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 8AMW	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6KXW Crystal structure of human aquaporin AQP7 in bound to glycerol Deposited 2019-09-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–342（342 aa） Chain B 1–342（342 aa） Chain C 1–342（342 aa） Chain D 1–342（342 aa）	Not recorded	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；277 K；30% v/v PEG 400, 50mM CAPS, pH 10.0, 0.16% w/v 1,5-Naphthalenedisulfonic acid disodium, 0.16% w/v Naphthalene-1,3,6-trisulfonic acid trisodium, 0.16% 1,4-piperazinediethanesulfonic acid	Resolution 3.70 Å R-free 0.322
6N1G Crystal structure of Aquaglyceroporin AQP7 Deposited 2018-11-08	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 × 4 PDB declaration: tetrameric	Chain A 1–342（342 aa） Chain C 1–342（342 aa）	Not recorded	GOL GLYCEROL × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；30% w/v polyethylene glycol 400, 100 mM MOPS pH 7.0, 100 mM NaCl.	Resolution 4.00 Å R-free 0.277
6N1G Crystal structure of Aquaglyceroporin AQP7 Deposited 2018-11-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 1–342（342 aa） Chain D 1–342（342 aa）	Not recorded	GOL GLYCEROL × 14	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；30% w/v polyethylene glycol 400, 100 mM MOPS pH 7.0, 100 mM NaCl.	Resolution 4.00 Å R-free 0.277
6QZI Crystal structure of human Aquaporin 7 at 1.9 A resolution Deposited 2019-03-11	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 × 4 PDB declaration: tetrameric	Chain A 33–279（247 aa）	Not recorded	GOL GLYCEROL × 56 PO4 PHOSPHATE ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；85 mM Tris pH 8.0, 37 % v/v PEG 200 and 0.80 % v/v OG	Resolution 1.90 Å R-free 0.195
6QZJ Crystal structure of human Aquaporin 7 at 2.2 A resolution Deposited 2019-03-11	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 × 4 PDB declaration: tetrameric	Chain A 33–279（247 aa）	Not recorded	GOL GLYCEROL × 44 PO4 PHOSPHATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；85 mM Tris pH 8.0, 37 % v/v PEG 200 and 0.80 % v/v OG	Resolution 2.20 Å R-free 0.243
8AMX AQP7 dimer of tetramers_D4 Deposited 2022-08-04	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–342（342 aa） Chain B 1–342（342 aa） Chain C 1–342（342 aa） Chain D 1–342（342 aa） Chain E 1–342（342 aa） Chain F 1–342（342 aa） Chain G 1–342（342 aa） Chain H 1–342（342 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；3s blot, 3s wait, 0s drain time, 0 blot force	Resolution 2.55 Å
8C9H AQP7_inhibitor Deposited 2023-01-22	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–342（342 aa） Chain B 1–342（342 aa） Chain C 1–342（342 aa） Chain D 1–342（342 aa） Chain E 1–342（342 aa） Chain F 1–342（342 aa） Chain G 1–342（342 aa） Chain H 1–342（342 aa）	Not recorded	T60 ethyl 4-[(4-pyrazol-1-ylphenyl)methylcarbamoylamino]benzoate × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；3s blot, 3s wait, 0s drain time, 0 blot force	Resolution 3.20 Å
8Y8V Cryo-EM structure of AQP7 in POPC nanodisc Deposited 2024-02-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–342（342 aa）	Not recorded	P5S O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.49 Å
8Y8V Cryo-EM structure of AQP7 in POPC nanodisc Deposited 2024-02-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–342（342 aa）	Not recorded	P5S O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.49 Å
8Y8V Cryo-EM structure of AQP7 in POPC nanodisc Deposited 2024-02-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–342（342 aa）	Not recorded	P5S O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.49 Å

7 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	AQP7_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–342； UniProt 1–342 Author chain B； PDBConstruct 1–342； UniProt 1–342 Author chain C； PDBConstruct 1–342； UniProt 1–342 Author chain D； PDBConstruct 1–342； UniProt 1–342 Author chain E； PDBConstruct 1–342； UniProt 1–342 Author chain F； PDBConstruct 1–342； UniProt 1–342 Author chain G； PDBConstruct 1–342； UniProt 1–342 Author chain H； PDBConstruct 1–342； UniProt 1–342

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	8amw
Deposition date deposition_date	2022-08-04
Structure title title	AQP7 dimer of tetramers_C1
Keywords keywords	membrane channel, octamer, adhesion protein, junction protein, MEMBRANE PROTEIN; MEMBRANE 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	40.13 Å
Radius of gyration Rg (electron density) rg_electron	39.91 Å
Forward intensity I(0) i0	615662000.00
Molecular weight molecular_weight	222820.0 kDa
Excluded volume excluded_volume	286570 Å³
Envelope volume envelope_volume	370390 Å³
Hydration-shell volume shell_volume	74758 Å³
Envelope diameter envelope_diameter	140.8 Å
Shell Rg shell_rg	47.56 Å
Envelope Rg envelope_rg	39.36 Å
Shape Rg shape_rg	39.89 Å
Total Rg total_rg	40.40 Å
Total atoms total_atoms	15734
Residues n_residues	2032
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	129.2 Å
Rg (real space) rg_real	40.03 Å
Rg uncertainty (real space) rg_real_error	0.98 Å
I(0) (real space) i0_real	6.1570e+08
I(0) uncertainty (real space) i0_real_error	1.1940e+07
Rg (reciprocal space) rg_reciprocal	40.13 Å
I(0) (reciprocal space) i0_reciprocal	615700000.0000
Solution quality estimate total_estimate	0.8935
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	46.4 Å
Skewness Skewness skewness	0.252
Kurtosis Kurtosis kurtosis	-0.448
Angular range angular_range	— – 0.1950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	82090000.0000
Real-space data points n_real_points	40
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.911

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Aquaporin-7
Molecular weight formula_weight	37264.4 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	15792

MVQASGHRRSTRGSKMVSWSVIAKIQEILQRKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGRISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYSLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNPALPGTEALVIGILVVIIGVSLGMNTGYAINPSRDLPPRIFTFIAGWGKQVFSNGENWWWVPVVAPLLGAYLGGIIYLVFIGSTIPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVSPANRSSVHPAPPLHESMALEHF

来源 Source

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	Komagataella pastoris

Entity 2 Entity 2 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	16

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	5

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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	3.00 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	102367

fit	/app/data/saxs_computation/am/8amw/8amw.fit
pddf	/app/data/pr_computation/am/8amw/8amw.pr.out
profile	/app/data/saxs_computation/am/8amw/8amw.dat

AQP7 dimer of tetramers_C1

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

Aquaporin-7

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