6d09

Crystal structure of PT2440 bound to HIF2a-B*:ARNT-B* complex

Method: X-RAY DIFFRACTION Dmax: 70.5 Å Quality: GOOD

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

Endothelial PAS domain-containing protein 1

Homo sapiens

UniProt Q99814

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 239–350 Fragment:residues 239-350 Mutation:R14E Aryl hydrocarbon receptor nuclear translocator × 1 (P27540) FOJ 3-{[(3R)-4-(difluoromethyl)-2,2-difluoro-3-hydroxy-1,1-dioxo-2,3-dihydro-1H-1-benzothiophen-5-yl]oxy}-5-fluorobenzonitrile × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.4;293 K;50 mM Bis-Tris pH5.4 and 16% PEG3350. Seeding with crushed crystals right after setup Resolution 1.85 Å R-free 0.282
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 239–350 Fragment:residues 239-350 Mutation:R14E Aryl hydrocarbon receptor nuclear translocator × 1 (P27540) FOJ 3-{[(3R)-4-(difluoromethyl)-2,2-difluoro-3-hydroxy-1,1-dioxo-2,3-dihydro-1H-1-benzothiophen-5-yl]oxy}-5-fluorobenzonitrile × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.4;293 K;50 mM Bis-Tris pH5.4 and 16% PEG3350. Seeding with crushed crystals right after setup Resolution 1.85 Å R-free 0.282

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.

41 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EPAS1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–117; UniProt 239–350

Aryl hydrocarbon receptor nuclear translocator

Homo sapiens

UniProt P27540

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 356–470 Fragment:residues 356-470 Mutation:E13R Endothelial PAS domain-containing protein 1 × 1 (Q99814) FOJ 3-{[(3R)-4-(difluoromethyl)-2,2-difluoro-3-hydroxy-1,1-dioxo-2,3-dihydro-1H-1-benzothiophen-5-yl]oxy}-5-fluorobenzonitrile × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.4;293 K;50 mM Bis-Tris pH5.4 and 16% PEG3350. Seeding with crushed crystals right after setup Resolution 1.85 Å R-free 0.282
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 356–470 Fragment:residues 356-470 Mutation:E13R Endothelial PAS domain-containing protein 1 × 1 (Q99814) FOJ 3-{[(3R)-4-(difluoromethyl)-2,2-difluoro-3-hydroxy-1,1-dioxo-2,3-dihydro-1H-1-benzothiophen-5-yl]oxy}-5-fluorobenzonitrile × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.4;293 K;50 mM Bis-Tris pH5.4 and 16% PEG3350. Seeding with crushed crystals right after setup Resolution 1.85 Å R-free 0.282

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.

42 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARNT_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 7–121; UniProt 356–470

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 6d09

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6d09
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6d09
Deposition date deposition_date2018-04-10
Structure title titleCrystal structure of PT2440 bound to HIF2a-B*:ARNT-B* complex
Keywords keywordsHif2a, Pas B domain, ARNT, hypoxia inducible factor, EPAS1, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.39
Radius of gyration Rg (electron density) rg_electron18.70
Forward intensity I(0) i012265700.00
Molecular weight molecular_weight25746.0 kDa
Excluded volume excluded_volume31962 ų
Envelope volume envelope_volume37312 ų
Hydration-shell volume shell_volume17107 ų
Envelope diameter envelope_diameter73.5
Shell Rg shell_rg24.53
Envelope Rg envelope_rg19.24
Shape Rg shape_rg18.68
Total Rg total_rg19.61
Total atoms total_atoms1807
Residues n_residues217
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 dmax70.5
Rg (real space) rg_real19.38
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.2270e+07
I(0) uncertainty (real space) i0_real_error1.6450e+05
Rg (reciprocal space) rg_reciprocal19.38
I(0) (reciprocal space) i0_reciprocal12270000.0000
Solution quality estimate total_estimate0.7627
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.9
Skewness Skewness skewness0.354
Kurtosis Kurtosis kurtosis-0.268
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2962000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.684; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.859; Smooth: 0.000

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_idd6d09a1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.110 — Profilin-like
Superfamily Superfamily superfamilyd.110.3 — PYP-like sensor domain (PAS domain)
Family Family familyd.110.3.7 — Hypoxia-inducible factor Hif2a, C-terminal domain
Domain ID domain_idd6d09a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6d09b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.110 — Profilin-like
Superfamily Superfamily superfamilyd.110.3 — PYP-like sensor domain (PAS domain)
Family Family familyd.110.3.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id6d09A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily20 — PAS domain
Domain ID domain_id6d09B01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily20 — PAS domain

8. Citations (1)

9. Files and Curves (10)