8w02

Q108K:K40L:T51V:T53S:R58W mutant of hCRBPII bound to synthetic fluorophore TD-1V

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–134 Mutation:Q108K:K40L:T51V:T53S:R58W ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;ammonium acetate, PEG 4000, sodium acetate Resolution 1.50 Å R-free 0.237
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–134 Mutation:Q108K:K40L:T51V:T53S:R58W ACT ACETATE ION × 1 A1AEQ (2E)-3-{5-[4-(dimethylamino)phenyl]thiophen-2-yl}but-2-enal × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;ammonium acetate, PEG 4000, sodium acetate Resolution 1.50 Å R-free 0.237

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 199 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 Author chain B; 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 8w02

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8w02
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8w02
Deposition date deposition_date2024-02-13
Structure title titleQ108K:K40L:T51V:T53S:R58W mutant of hCRBPII bound to synthetic fluorophore TD-1V
Keywords keywordshuman cellular retinol binding protein II, hCRBPII, TD-1V, engineered protein, fluorescent protein, RETINOL BINDING PROTEIN; RETINOL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.79
Radius of gyration Rg (electron density) rg_electron21.00
Forward intensity I(0) i016186400.00
Molecular weight molecular_weight29991.0 kDa
Excluded volume excluded_volume37289 ų
Envelope volume envelope_volume44352 ų
Hydration-shell volume shell_volume18512 ų
Envelope diameter envelope_diameter71.7
Shell Rg shell_rg26.21
Envelope Rg envelope_rg21.06
Shape Rg shape_rg21.01
Total Rg total_rg21.69
Total atoms total_atoms2116
Residues n_residues266
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_real21.87
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.6190e+07
I(0) uncertainty (real space) i0_real_error2.0700e+05
Rg (reciprocal space) rg_reciprocal21.86
I(0) (reciprocal space) i0_reciprocal16190000.0000
Solution quality estimate total_estimate0.8788
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.423
Kurtosis Kurtosis kurtosis-0.405
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3784000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.932; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)