9pt1

Q108K:K40L:T51V:T53S:R58W:Y19W:L117E mutant of hCRBPII bound to fluorophore TD-1V-10

Method: X-RAY DIFFRACTION Dmax: 47.5 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:Y19W:L117E A1CK0 (2E)-3-{4-[5-(dimethylamino)thiophen-2-yl]phenyl}but-2-enal × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;PEG4000, ammonium acetate, 100 mM sodium acetate, pH 4.0 - 4.8 Resolution 1.48 Å R-free 0.195

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 9pt1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9pt1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9pt1
Deposition date deposition_date2025-07-27
最后修订 last_revision2025-10-01
Structure title titleQ108K:K40L:T51V:T53S:R58W:Y19W:L117E mutant of hCRBPII bound to fluorophore TD-1V-10
Keywords keywordshuman cellular retinol binding protein II, hCRBPII, fluorescent protein, engineered 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_guinier15.20
Radius of gyration Rg (electron density) rg_electron14.04
Forward intensity I(0) i08855710.00
Molecular weight molecular_weight14836.0 kDa
Excluded volume excluded_volume14422 ų
Envelope volume envelope_volume21858 ų
Hydration-shell volume shell_volume13049 ų
Envelope diameter envelope_diameter46.6
Shell Rg shell_rg20.06
Envelope Rg envelope_rg14.31
Shape Rg shape_rg13.96
Total Rg total_rg15.05
Total atoms total_atoms1138
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 dmax47.5
Rg (real space) rg_real15.08
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real8.8560e+06
I(0) uncertainty (real space) i0_real_error9.8490e+04
Rg (reciprocal space) rg_reciprocal15.09
I(0) (reciprocal space) i0_reciprocal8856000.0000
Solution quality estimate total_estimate0.8940
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.8
Skewness Skewness skewness0.114
Kurtosis Kurtosis kurtosis-0.427
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1611000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)