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6n1g

Crystal structure of Aquaglyceroporin AQP7

Method: X-RAY DIFFRACTION Dmax: 116.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Aquaporin-7

Homo sapiens

UniProt O14520

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 1–342 Chain C； UniProt 1–342 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
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain B； UniProt 1–342 Chain D； UniProt 1–342 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

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 6N1G 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 ligand/ion 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
6QZI Crystal structure of human Aquaporin 7 at 1.9 A resolution Deposited 2019-03-11 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 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 ligand/ion 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
8AMW AQP7 dimer of tetramers_C1 Deposited 2022-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein 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 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
8AMX AQP7 dimer of tetramers_D4 Deposited 2022-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein 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 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 × 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 method 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 method 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 method 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 9 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

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.

SAXS scattering curve SAXS Profile

SAXS profile for 6n1g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6n1g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6n1g
Deposition date deposition_date2018-11-08
Structure title titleCrystal structure of Aquaglyceroporin AQP7
Keywords keywordsAquaglyceroporin, water, glycerol, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier34.87 Å
Radius of gyration Rg (electron density) rg_electron34.84 Å
Forward intensity I(0) i0152865000.00
Molecular weight molecular_weight109020.0 kDa
Excluded volume excluded_volume140190 ų
Envelope volume envelope_volume171870 ų
Hydration-shell volume shell_volume41780 ų
Envelope diameter envelope_diameter117.7 Å
Shell Rg shell_rg40.50 Å
Envelope Rg envelope_rg34.71 Å
Shape Rg shape_rg34.82 Å
Total Rg total_rg35.33 Å
Total atoms total_atoms15472
Residues n_residues996
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax116.8 Å
Rg (real space) rg_real35.01 Å
Rg uncertainty (real space) rg_real_error1.07 Å
I(0) (real space) i0_real1.5290e+08
I(0) uncertainty (real space) i0_real_error2.6090e+06
Rg (reciprocal space) rg_reciprocal34.93 Å
I(0) (reciprocal space) i0_reciprocal152900000.0000
Solution quality estimate total_estimate0.6918
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.8 Å
Skewness Skewness skewness0.396
Kurtosis Kurtosis kurtosis-0.499
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27610000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 0.186; Positv: 1.000; Valcen: 0.908; Smooth: 0.910
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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) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6n1gA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1080 — Glycerol uptake facilitator protein
Homologous superfamily homologous superfamily10 — Glycerol uptake facilitator protein.
Domain ID domain_id6n1gB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1080 — Glycerol uptake facilitator protein
Homologous superfamily homologous superfamily10 — Glycerol uptake facilitator protein.
Domain ID domain_id6n1gC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1080 — Glycerol uptake facilitator protein
Homologous superfamily homologous superfamily10 — Glycerol uptake facilitator protein.
Domain ID domain_id6n1gD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1080 — Glycerol uptake facilitator protein
Homologous superfamily homologous superfamily10 — Glycerol uptake facilitator protein.
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8. Citations (1)

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9. Files and Curves (10)