6e50

Crystal structure of the apo domain-swapped dimer Q108K:K40L:T51F mutant of human Cellular Retinol Binding Protein II

Method: X-RAY DIFFRACTION Dmax: 69.9 Å Quality: EXCELLENT

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, K40L, T51F ACT ACETATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;298 K;PEG 4000, sodium acetate, Ammonium acetate Resolution 1.97 Å R-free 0.266

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 6e50

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6e50
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6e50
Deposition date deposition_date2018-07-18
Structure title titleCrystal structure of the apo domain-swapped dimer Q108K:K40L:T51F mutant of human Cellular Retinol Binding Protein II
Keywords keywordsRetinol, iLBP, Protein Switch, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.68
Radius of gyration Rg (electron density) rg_electron20.76
Forward intensity I(0) i04813480.00
Molecular weight molecular_weight15705.0 kDa
Excluded volume excluded_volume19545 ų
Envelope volume envelope_volume27900 ų
Hydration-shell volume shell_volume12329 ų
Envelope diameter envelope_diameter68.9
Shell Rg shell_rg25.07
Envelope Rg envelope_rg20.37
Shape Rg shape_rg20.78
Total Rg total_rg21.43
Total atoms total_atoms1106
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 dmax69.9
Rg (real space) rg_real21.77
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real4.8130e+06
I(0) uncertainty (real space) i0_real_error6.9230e+04
Rg (reciprocal space) rg_reciprocal21.75
I(0) (reciprocal space) i0_reciprocal4813000.0000
Solution quality estimate total_estimate0.9002
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.9
Skewness Skewness skewness0.293
Kurtosis Kurtosis kurtosis-0.543
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha299000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.969; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.853; Smooth: 0.939

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_idd6e50a_
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_id6e50A00
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)