1jyd

Crystal Structure of Recombinant Human Serum Retinol-Binding Protein at 1.7 A Resolution

Method: X-RAY DIFFRACTION Dmax: 53.3 Å Quality: GOOD

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

PLASMA RETINOL-BINDING PROTEIN

Homo sapiens

UniProt P02753

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 17–198 Not recorded GOL GLYCEROL × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;289 K;Sodium cacodylate, sodium chloride, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 1.70 Å R-free 0.270

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.

22 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RETBP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–183; UniProt 17–198

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 1jyd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jyd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1jyd
Deposition date deposition_date2001-09-12
Structure title titleCrystal Structure of Recombinant Human Serum Retinol-Binding Protein at 1.7 A Resolution
Keywords keywordsretinol binding protein, lipocalin superfamily, beta barrel, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.71
Radius of gyration Rg (electron density) rg_electron15.49
Forward intensity I(0) i08422340.00
Molecular weight molecular_weight20562.0 kDa
Excluded volume excluded_volume25413 ų
Envelope volume envelope_volume28795 ų
Hydration-shell volume shell_volume15325 ų
Envelope diameter envelope_diameter52.0
Shell Rg shell_rg21.73
Envelope Rg envelope_rg16.08
Shape Rg shape_rg15.47
Total Rg total_rg16.64
Total atoms total_atoms1443
Residues n_residues174
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 dmax53.3
Rg (real space) rg_real16.60
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real8.4220e+06
I(0) uncertainty (real space) i0_real_error8.0490e+04
Rg (reciprocal space) rg_reciprocal16.61
I(0) (reciprocal space) i0_reciprocal8422000.0000
Solution quality estimate total_estimate0.8898
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.115
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.4750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1795000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.996

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_idd1jyda_
Class classb — All beta proteins
Fold Fold foldb.60 — Lipocalins
Superfamily Superfamily superfamilyb.60.1 — Lipocalins
Family Family familyb.60.1.1 — Retinol binding protein-like

CATH v4.4 (1 domains)

Domain ID domain_id1jydA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily20 — Calycin beta-barrel core domain

8. Citations (3)

9. Files and Curves (10)