3fmz

Crystal Structure of Retinol-Binding Protein 4 (RBP4) in complex with non-retinoid ligand

Method: X-RAY DIFFRACTION Dmax: 87.1 Å Quality: GOOD

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

Retinol-binding protein 4

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 19–201 Not recorded 2T1 2-[({4-[2-(trifluoromethyl)phenyl]piperidin-1-yl}carbonyl)amino]benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;289 K;0.4M Mg formate, 0.1M GndHCl, 0.1M Bis-Tris 6.5, vapor diffusion, temperature 289K Resolution 2.90 Å R-free 0.286
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 19–201 Not recorded 2T1 2-[({4-[2-(trifluoromethyl)phenyl]piperidin-1-yl}carbonyl)amino]benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;289 K;0.4M Mg formate, 0.1M GndHCl, 0.1M Bis-Tris 6.5, vapor diffusion, temperature 289K Resolution 2.90 Å R-free 0.286

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 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RET4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 30–212; UniProt 19–201 Author chain B; PDBConstruct 30–212; UniProt 19–201

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 3fmz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3fmz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3fmz
Deposition date deposition_date2008-12-22
Structure title titleCrystal Structure of Retinol-Binding Protein 4 (RBP4) in complex with non-retinoid ligand
Keywords keywordsretinol binding, Disease mutation, Retinol-binding, Secreted, Sensory transduction, Transport, Vision, Vitamin A, 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_guinier25.06
Radius of gyration Rg (electron density) rg_electron24.51
Forward intensity I(0) i030010200.00
Molecular weight molecular_weight40804.0 kDa
Excluded volume excluded_volume50419 ų
Envelope volume envelope_volume62794 ų
Hydration-shell volume shell_volume22300 ų
Envelope diameter envelope_diameter91.4
Shell Rg shell_rg30.31
Envelope Rg envelope_rg24.68
Shape Rg shape_rg24.47
Total Rg total_rg25.31
Total atoms total_atoms2870
Residues n_residues348
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 dmax87.1
Rg (real space) rg_real25.19
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real3.0010e+07
I(0) uncertainty (real space) i0_real_error4.1080e+05
Rg (reciprocal space) rg_reciprocal25.15
I(0) (reciprocal space) i0_reciprocal30010000.0000
Solution quality estimate total_estimate0.8451
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.491
Kurtosis Kurtosis kurtosis-0.280
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6741000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.744; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.764; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3fmza_
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
Domain ID domain_idd3fmzb_
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 (2 domains)

Domain ID domain_id3fmzA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily20 — Calycin beta-barrel core domain
Domain ID domain_id3fmzB00
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)