7ucv

The Crystal Structure of Apo Domain-Swapped Dimer Q108K:T51D:A28CL36C R58:H:H:H:N59 HCRBPII with Histidine Insertion in the Hinge Loop Region at 2.19 Angstrom Resolution

Method: X-RAY DIFFRACTION Dmax: 80.9 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 Chain B; UniProt 2–134 Mutation:A28C, L36C, T51D, Q111K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;PEG 4000, sodium acetate, ammonium acetate Resolution 2.19 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 1–136; UniProt 2–134 Author chain B; PDBConstruct 1–136; 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 7ucv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ucv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ucv
Deposition date deposition_date2022-03-17
Structure title titleThe Crystal Structure of Apo Domain-Swapped Dimer Q108K:T51D:A28CL36C R58:H:H:H:N59 HCRBPII with Histidine Insertion in the Hinge Loop Region at 2.19 Angstrom Resolution
Keywords keywordsLBP, CRBPII, 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_guinier25.44
Radius of gyration Rg (electron density) rg_electron25.15
Forward intensity I(0) i019014600.00
Molecular weight molecular_weight32006.0 kDa
Excluded volume excluded_volume39492 ų
Envelope volume envelope_volume49705 ų
Hydration-shell volume shell_volume17877 ų
Envelope diameter envelope_diameter81.6
Shell Rg shell_rg30.26
Envelope Rg envelope_rg24.87
Shape Rg shape_rg25.19
Total Rg total_rg25.66
Total atoms total_atoms2250
Residues n_residues272
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 dmax80.9
Rg (real space) rg_real25.66
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.9010e+07
I(0) uncertainty (real space) i0_real_error2.3790e+05
Rg (reciprocal space) rg_reciprocal25.60
I(0) (reciprocal space) i0_reciprocal19010000.0000
Solution quality estimate total_estimate0.8117
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.446
Kurtosis Kurtosis kurtosis-0.697
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4668000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.655; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.742; Smooth: 0.841

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)