2qm9

Troglitazone Bound to Fatty Acid Binding Protein 4

Method: X-RAY DIFFRACTION Dmax: 62.6 Å Quality: EXCELLENT

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

Fatty acid-binding protein, adipocyte

Mus musculus

UniProt P04117

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–132 Chain B; UniProt 1–132 Not recorded SO4 SULFATE ION × 3 TDZ (5R)-5-(4-{[(2R)-6-HYDROXY-2,5,7,8-TETRAMETHYL-3,4-DIHYDRO-2H-CHROMEN-2-YL]METHOXY}BENZYL)-1,3-THIAZOLIDINE-2,4-DIONE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:hanging drop;pH 4.5;298 K;1.6 M ammonium sulfate, 0.1 M sodium acetate, 0.05 M K/Na phosphate, pH 4.5, hanging drop, temperature 298K Resolution 2.31 Å R-free 0.276

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 FABPA_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–155; UniProt 1–132 Author chain B; PDBConstruct 24–155; UniProt 1–132

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 2qm9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2qm9
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2qm9
Deposition date deposition_date2007-07-14
Structure title titleTroglitazone Bound to Fatty Acid Binding Protein 4
Keywords keywordsbeta clamshell, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.38
Radius of gyration Rg (electron density) rg_electron19.34
Forward intensity I(0) i016953000.00
Molecular weight molecular_weight30832.0 kDa
Excluded volume excluded_volume38506 ų
Envelope volume envelope_volume45244 ų
Hydration-shell volume shell_volume19676 ų
Envelope diameter envelope_diameter62.6
Shell Rg shell_rg25.53
Envelope Rg envelope_rg19.39
Shape Rg shape_rg19.30
Total Rg total_rg20.31
Total atoms total_atoms2153
Residues n_residues271
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 dmax62.6
Rg (real space) rg_real20.31
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real1.6950e+07
I(0) uncertainty (real space) i0_real_error2.0590e+05
Rg (reciprocal space) rg_reciprocal20.32
I(0) (reciprocal space) i0_reciprocal16950000.0000
Solution quality estimate total_estimate0.9092
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.225
Kurtosis Kurtosis kurtosis-0.516
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3972000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2qm9a2
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_idd2qm9a3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2qm9b_
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 (2 domains)

Domain ID domain_id2qm9A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily20 — Calycin beta-barrel core domain
Domain ID domain_id2qm9B00
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)