2rct

Crystal structure of human holo cellular retinol-binding protein II (CRBP-II)

Method: X-RAY DIFFRACTION Dmax: 49.1 Å Quality: GOOD

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

Retinol-binding protein II, cellular

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 Not recorded SO4 SULFATE ION × 2 RTL RETINOL × 1 TLA L(+)-TARTARIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;293 K;0.1 M sodium citrate, 0.2 M sodium/potassium tartrate, 1.4 M ammonium sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.20 Å R-free 0.215

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 5–137; 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 2rct

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2rct
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2rct
Deposition date deposition_date2007-09-20
Structure title titleCrystal structure of human holo cellular retinol-binding protein II (CRBP-II)
Keywords keywords;cellular retinol-binding protein II, CRBP II, retinol, lipid-binding protein, Cytoplasm, Transport, Vitamin A, 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_guinier15.87
Radius of gyration Rg (electron density) rg_electron14.44
Forward intensity I(0) i05911090.00
Molecular weight molecular_weight17100.0 kDa
Excluded volume excluded_volume21201 ų
Envelope volume envelope_volume23658 ų
Hydration-shell volume shell_volume13696 ų
Envelope diameter envelope_diameter48.8
Shell Rg shell_rg20.48
Envelope Rg envelope_rg14.68
Shape Rg shape_rg14.40
Total Rg total_rg15.66
Total atoms total_atoms1199
Residues n_residues141
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 dmax49.1
Rg (real space) rg_real15.74
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real5.9110e+06
I(0) uncertainty (real space) i0_real_error6.0090e+04
Rg (reciprocal space) rg_reciprocal15.76
I(0) (reciprocal space) i0_reciprocal5911000.0000
Solution quality estimate total_estimate0.8982
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.5
Skewness Skewness skewness0.074
Kurtosis Kurtosis kurtosis-0.439
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1129000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2rcta1
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
Domain ID domain_idd2rcta2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2rcta3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2rctA00
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)