4qyp

The Crystal Structures of holo-wt human Cellular Retinol Binding protein II (hCRBPII) bound to Retinal

Method: X-RAY DIFFRACTION Dmax: 81.8 Å Quality: EXCELLENT

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 Fragment:transfer protein RET RETINAL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 4.6;298 K;30% PEG 4000, 0.1 M sodium acetate, 0.1 M ammonium acetate , pH 4.6, EVAPORATION, temperature 298K Resolution 1.62 Å R-free 0.252
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–134 Fragment:transfer protein RET RETINAL × 1 ACT ACETATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 4.6;298 K;30% PEG 4000, 0.1 M sodium acetate, 0.1 M ammonium acetate , pH 4.6, EVAPORATION, temperature 298K Resolution 1.62 Å R-free 0.252
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 2–134 Fragment:transfer protein RET RETINAL × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 4.6;298 K;30% PEG 4000, 0.1 M sodium acetate, 0.1 M ammonium acetate , pH 4.6, EVAPORATION, temperature 298K Resolution 1.62 Å R-free 0.252
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 2–134 Fragment:transfer protein ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 4.6;298 K;30% PEG 4000, 0.1 M sodium acetate, 0.1 M ammonium acetate , pH 4.6, EVAPORATION, temperature 298K Resolution 1.62 Å R-free 0.252

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 197 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 Author chain C; PDBConstruct 1–133; UniProt 2–134 Author chain D; 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 4qyp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4qyp
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4qyp
Deposition date deposition_date2014-07-25
Structure title titleThe Crystal Structures of holo-wt human Cellular Retinol Binding protein II (hCRBPII) bound to Retinal
Keywords keywordsbeta barrel, transfer protein, kidney, liver, RETINOL-BINDING PROT, 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_guinier26.64
Radius of gyration Rg (electron density) rg_electron25.53
Forward intensity I(0) i066133400.00
Molecular weight molecular_weight62298.0 kDa
Excluded volume excluded_volume77440 ų
Envelope volume envelope_volume93690 ų
Hydration-shell volume shell_volume30332 ų
Envelope diameter envelope_diameter84.1
Shell Rg shell_rg33.10
Envelope Rg envelope_rg25.40
Shape Rg shape_rg25.54
Total Rg total_rg26.31
Total atoms total_atoms4390
Residues n_residues532
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 dmax81.8
Rg (real space) rg_real26.52
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real6.6130e+07
I(0) uncertainty (real space) i0_real_error8.3420e+05
Rg (reciprocal space) rg_reciprocal26.56
I(0) (reciprocal space) i0_reciprocal66140000.0000
Solution quality estimate total_estimate0.9114
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary79.1
Skewness Skewness skewness0.160
Kurtosis Kurtosis kurtosis-0.566
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18010000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4qypa_
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_idd4qypb_
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_idd4qypc_
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_idd4qypd_
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

CATH v4.4 (4 domains)

Domain ID domain_id4qypA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily20 — Calycin beta-barrel core domain
Domain ID domain_id4qypB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily20 — Calycin beta-barrel core domain
Domain ID domain_id4qypC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily20 — Calycin beta-barrel core domain
Domain ID domain_id4qypD00
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)