6e5e

Crystal structure of the apo domain-swapped dimer Q108K:T51D mutant of human cellular retinol binding protein II

Method: X-RAY DIFFRACTION Dmax: 71.3 Å Quality: GOOD

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

Retinol-binding protein 2

Homo sapiens

UniProt P50120

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–134 Mutation:Q108K, T51D ACT ACETATE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;4000 PEG, sodium acetate, ammonium acetate Resolution 1.70 Å R-free 0.242

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.

101 other PDB entries and 200 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RET2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–133; UniProt 2–134

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 6e5e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6e5e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6e5e
Deposition date deposition_date2018-07-20
Structure title titleCrystal structure of the apo domain-swapped dimer Q108K:T51D mutant of human cellular retinol binding protein II
Keywords keywordsRetinol, iLBP, Protein Switch, CYTOSOLIC PROTEIN, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.49
Radius of gyration Rg (electron density) rg_electron20.57
Forward intensity I(0) i04953050.00
Molecular weight molecular_weight15669.0 kDa
Excluded volume excluded_volume19379 ų
Envelope volume envelope_volume27292 ų
Hydration-shell volume shell_volume12195 ų
Envelope diameter envelope_diameter69.1
Shell Rg shell_rg24.93
Envelope Rg envelope_rg20.27
Shape Rg shape_rg20.59
Total Rg total_rg21.26
Total atoms total_atoms1102
Residues n_residues133
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 dmax71.3
Rg (real space) rg_real21.58
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real4.9530e+06
I(0) uncertainty (real space) i0_real_error7.5820e+04
Rg (reciprocal space) rg_reciprocal21.56
I(0) (reciprocal space) i0_reciprocal4953000.0000
Solution quality estimate total_estimate0.8955
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.302
Kurtosis Kurtosis kurtosis-0.547
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha313600.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.830; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6e5ea_
Class classb — All beta proteins
Fold Fold foldb.60 — Lipocalins
Superfamily Superfamily superfamilyb.60.1 — Lipocalins
Family Family familyb.60.1.2 — Fatty acid binding protein-like

CATH v4.4 (1 domains)

Domain ID domain_id6e5eA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily20 — Calycin beta-barrel core domain

8. Citations (1)

9. Files and Curves (10)