2npa

the crystal structure of the human PPARaplpha ligand binding domain in complex with a a-hydroxyimino phenylpropanoic acid

Method: X-RAY DIFFRACTION Dmax: 99.7 Å Quality: GOOD

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

Peroxisome proliferator-activated receptor alpha

Homo sapiens

UniProt Q07869

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 199–468 Fragment:ligand binding domain SRC- peptide from Nuclear receptor coactivator 1 × 1 (Q2T9G5) MMB (2R,3E)-2-{4-[(5-METHYL-2-PHENYL-1,3-OXAZOL-4-YL)METHOXY]BENZYL}-3-(PROPOXYIMINO)BUTANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;6% PEG 10K. 0.1M Hepes, 6% ethylene glycol, pH 7.5, VAPOR DIFFUSION, HANGING DROP Resolution 2.30 Å R-free 0.260
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 199–468 Fragment:ligand binding domain SRC- peptide from Nuclear receptor coactivator 1 × 1 (Q2T9G5) MMB (2R,3E)-2-{4-[(5-METHYL-2-PHENYL-1,3-OXAZOL-4-YL)METHOXY]BENZYL}-3-(PROPOXYIMINO)BUTANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;6% PEG 10K. 0.1M Hepes, 6% ethylene glycol, pH 7.5, VAPOR DIFFUSION, HANGING DROP Resolution 2.30 Å R-free 0.260

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.

78 other PDB entries and 105 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPARA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–270; UniProt 199–468 Author chain C; PDBConstruct 1–270; UniProt 199–468

SRC- peptide from Nuclear receptor coactivator 1

OrganismNot specified

UniProt Q2T9G5

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 683–697 Not recorded Peroxisome proliferator-activated receptor alpha × 1 (Q07869) MMB (2R,3E)-2-{4-[(5-METHYL-2-PHENYL-1,3-OXAZOL-4-YL)METHOXY]BENZYL}-3-(PROPOXYIMINO)BUTANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;6% PEG 10K. 0.1M Hepes, 6% ethylene glycol, pH 7.5, VAPOR DIFFUSION, HANGING DROP Resolution 2.30 Å R-free 0.260
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 683–697 Not recorded Peroxisome proliferator-activated receptor alpha × 1 (Q07869) MMB (2R,3E)-2-{4-[(5-METHYL-2-PHENYL-1,3-OXAZOL-4-YL)METHOXY]BENZYL}-3-(PROPOXYIMINO)BUTANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;6% PEG 10K. 0.1M Hepes, 6% ethylene glycol, pH 7.5, VAPOR DIFFUSION, HANGING DROP Resolution 2.30 Å R-free 0.260

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2T9G5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–15; UniProt 683–697 Author chain D; PDBConstruct 1–15; UniProt 683–697

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 2npa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2npa
Deposition date deposition_date2006-10-26
Structure title titlethe crystal structure of the human PPARaplpha ligand binding domain in complex with a a-hydroxyimino phenylpropanoic acid
Keywords keywordsprotein-agonist complex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.68
Radius of gyration Rg (electron density) rg_electron30.15
Forward intensity I(0) i062635600.00
Molecular weight molecular_weight64391.0 kDa
Excluded volume excluded_volume81593 ų
Envelope volume envelope_volume100350 ų
Hydration-shell volume shell_volume28856 ų
Envelope diameter envelope_diameter102.6
Shell Rg shell_rg35.76
Envelope Rg envelope_rg30.02
Shape Rg shape_rg30.14
Total Rg total_rg30.71
Total atoms total_atoms4516
Residues n_residues561
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 dmax99.7
Rg (real space) rg_real30.84
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real6.2640e+07
I(0) uncertainty (real space) i0_real_error9.0520e+05
Rg (reciprocal space) rg_reciprocal30.77
I(0) (reciprocal space) i0_reciprocal62630000.0000
Solution quality estimate total_estimate0.8646
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.402
Kurtosis Kurtosis kurtosis-0.611
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha20940000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.840; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.842; Smooth: 0.873

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2npaa_
Class classa — All alpha proteins
Fold Fold folda.123 — Nuclear receptor ligand-binding domain
Superfamily Superfamily superfamilya.123.1 — Nuclear receptor ligand-binding domain
Family Family familya.123.1.1 — Nuclear receptor ligand-binding domain
Domain ID domain_idd2npac_
Class classa — All alpha proteins
Fold Fold folda.123 — Nuclear receptor ligand-binding domain
Superfamily Superfamily superfamilya.123.1 — Nuclear receptor ligand-binding domain
Family Family familya.123.1.1 — Nuclear receptor ligand-binding domain

CATH v4.4 (2 domains)

Domain ID domain_id2npaA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id2npaC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor

8. Citations (1)

9. Files and Curves (10)