6poj

STRUCTURAL REFINEMENT OF AQUAPORIN 1 VIA SSNMR

Method: SOLID-STATE NMR Dmax: 83.5 Å Quality: REASONABLE

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

Aquaporin-1

Homo sapiens

UniProt P29972

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–269 Not recorded No other associated polymer 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

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.

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

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 6poj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6poj
Deposition date deposition_date2019-07-04
Structure title titleSTRUCTURAL REFINEMENT OF AQUAPORIN 1 VIA SSNMR
Keywords keywordsTRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodSOLID-STATE NMR

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

Radius of gyration Rg (Guinier) rg_guinier30.46
Radius of gyration Rg (electron density) rg_electron29.48
Forward intensity I(0) i01307130000.00
Molecular weight molecular_weight312010.0 kDa
Excluded volume excluded_volume394150 ų
Envelope volume envelope_volume258430 ų
Hydration-shell volume shell_volume52596 ų
Envelope diameter envelope_diameter144.3
Shell Rg shell_rg44.99
Envelope Rg envelope_rg43.08
Shape Rg shape_rg29.51
Total Rg total_rg29.85
Total atoms total_atoms44170
Residues n_residues2920
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 dmax83.5
Rg (real space) rg_real28.68
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real1.2510e+09
I(0) uncertainty (real space) i0_real_error1.5360e+07
Rg (reciprocal space) rg_reciprocal30.81
I(0) (reciprocal space) i0_reciprocal1307000000.0000
Solution quality estimate total_estimate0.6037
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary22.5
Skewness Skewness skewness0.476
Kurtosis Kurtosis kurtosis-0.743
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha1.9470
Highest regularization parameter α highest_alpha3361000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.790; Stabil: 0.970; Sysdev: 0.000; Positv: 1.000; Valcen: 0.578; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6pojA00
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)