3h7w

Crystal structure of the high affinity heterodimer of HIF2 alpha and ARNT C-terminal PAS domains with the artificial ligand THS017

Method: X-RAY DIFFRACTION Dmax: 63.4 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:HIF2alpha C-terminal PAS domain (UNP residues 239 to 350) Mutation:R247E Aryl hydrocarbon receptor nuclear translocator × 1 (P27540) 018 2-nitro-N-(thiophen-3-ylmethyl)-4-(trifluoromethyl)aniline × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;0.1M BisTris, 17% PEG3350, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.65 Å R-free 0.236

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 46 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:ARNT C-terminal PAS domain (UNP residues 356 to 470) Mutation:E362R Endothelial PAS domain-containing protein 1 × 1 (Q99814) 018 2-nitro-N-(thiophen-3-ylmethyl)-4-(trifluoromethyl)aniline × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;0.1M BisTris, 17% PEG3350, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.65 Å R-free 0.236

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 48 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 3h7w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3h7w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3h7w
Deposition date deposition_date2009-04-28
Structure title titleCrystal structure of the high affinity heterodimer of HIF2 alpha and ARNT C-terminal PAS domains with the artificial ligand THS017
Keywords keywords;PAS domain, heterodimer, protein ligand complex., Activator, Angiogenesis, Congenital erythrocytosis, Developmental protein, Differentiation, Disease mutation, DNA-binding, Hydroxylation, Nucleus, Phosphoprotein, Transcription, Transcription regulation, Ubl conjugation, Alternative splicing, Polymorphism ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.48
Radius of gyration Rg (electron density) rg_electron17.70
Forward intensity I(0) i022284900.00
Molecular weight molecular_weight24044.0 kDa
Excluded volume excluded_volume23210 ų
Envelope volume envelope_volume36437 ų
Hydration-shell volume shell_volume17353 ų
Envelope diameter envelope_diameter62.5
Shell Rg shell_rg23.68
Envelope Rg envelope_rg18.01
Shape Rg shape_rg17.71
Total Rg total_rg18.35
Total atoms total_atoms1811
Residues n_residues218
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 dmax63.4
Rg (real space) rg_real18.44
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real2.2280e+07
I(0) uncertainty (real space) i0_real_error2.7630e+05
Rg (reciprocal space) rg_reciprocal18.44
I(0) (reciprocal space) i0_reciprocal22280000.0000
Solution quality estimate total_estimate0.7899
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.8
Skewness Skewness skewness0.330
Kurtosis Kurtosis kurtosis-0.286
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5708000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.761; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; 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_idd3h7wa1
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_idd3h7wa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3h7wb_
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_id3h7wA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily20 — PAS domain
Domain ID domain_id3h7wB01
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)