6qzi

Crystal structure of human Aquaporin 7 at 1.9 A resolution

Method: X-RAY DIFFRACTION Dmax: 63.3 Å Quality: GOOD

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 33–279 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

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.

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 1–247; UniProt 33–279

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 6qzi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6qzi
Deposition date deposition_date2019-03-11
Structure title titleCrystal structure of human Aquaporin 7 at 1.9 A resolution
Keywords keywordsAquaglyceroporin, glycerol channel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.88
Radius of gyration Rg (electron density) rg_electron17.85
Forward intensity I(0) i012605900.00
Molecular weight molecular_weight28218.0 kDa
Excluded volume excluded_volume36002 ų
Envelope volume envelope_volume39630 ų
Hydration-shell volume shell_volume18418 ų
Envelope diameter envelope_diameter64.6
Shell Rg shell_rg24.26
Envelope Rg envelope_rg18.37
Shape Rg shape_rg17.82
Total Rg total_rg18.97
Total atoms total_atoms1982
Residues n_residues247
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax63.3
Rg (real space) rg_real18.85
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.2610e+07
I(0) uncertainty (real space) i0_real_error1.6710e+05
Rg (reciprocal space) rg_reciprocal18.85
I(0) (reciprocal space) i0_reciprocal12610000.0000
Solution quality estimate total_estimate0.7989
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.9
Skewness Skewness skewness0.353
Kurtosis Kurtosis kurtosis-0.192
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2370000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.797; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6qziA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1080 — Glycerol uptake facilitator protein
Homologous superfamily homologous superfamily10 — Glycerol uptake facilitator protein.

8. Citations (1)

9. Files and Curves (10)