2a24

HADDOCK Structure of HIF-2a/ARNT PAS-B Heterodimer

Method: SOLUTION NMR Dmax: 55.2 Å Quality: GOOD

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

Endothelial PAS domain protein 1

OrganismNot specified

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 242–348 Fragment:C-terminal PAS domain (PAS-B) Aryl hydrocarbon receptor nuclear translocator × 1 (P27540) SOLUTION NMR NMR measurement conditions:pH 7.5;Ionic strength (raw mmCIF value) 50mM Tris, 17mM NaCl, 5mM DTT NMR sample composition:250 micro M (15N)HIF-2alpha PAS-B (240-350) + 1mM ARNT PAS-B (356-470), 50mM Tris (pH=7.5), 17mM NaCl, 5mM DTT NMR sample composition:250 micro M (15N)ARNT PAS-B (356-470) + 1mM HIF-2alpha PAS-B (240-350), 50mM Tris (pH=7.5), 17mM NaCl, 5mM DTT Resolution not provided

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 1–107; UniProt 242–348

Aryl hydrocarbon receptor nuclear translocator

OrganismNot specified

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 358–465 Fragment:C-terminal PAS domain (PAS-B) Endothelial PAS domain protein 1 × 1 (Q99814) SOLUTION NMR NMR measurement conditions:pH 7.5;Ionic strength (raw mmCIF value) 50mM Tris, 17mM NaCl, 5mM DTT NMR sample composition:250 micro M (15N)HIF-2alpha PAS-B (240-350) + 1mM ARNT PAS-B (356-470), 50mM Tris (pH=7.5), 17mM NaCl, 5mM DTT NMR sample composition:250 micro M (15N)ARNT PAS-B (356-470) + 1mM HIF-2alpha PAS-B (240-350), 50mM Tris (pH=7.5), 17mM NaCl, 5mM DTT Resolution not provided

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 1–108; UniProt 358–465

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 2a24

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2a24
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2a24
Deposition date deposition_date2005-06-21
Structure title titleHADDOCK Structure of HIF-2a/ARNT PAS-B Heterodimer
Keywords keywordsARNT, HIF, hypoxia, transcription, PAS; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.50
Radius of gyration Rg (electron density) rg_electron17.38
Forward intensity I(0) i03609950000.00
Molecular weight molecular_weight505600.0 kDa
Excluded volume excluded_volume628940 ų
Envelope volume envelope_volume55165 ų
Hydration-shell volume shell_volume23286 ų
Envelope diameter envelope_diameter61.4
Shell Rg shell_rg26.44
Envelope Rg envelope_rg19.27
Shape Rg shape_rg17.39
Total Rg total_rg17.43
Total atoms total_atoms70040
Residues n_residues4300
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 dmax55.2
Rg (real space) rg_real17.46
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real3.6100e+09
I(0) uncertainty (real space) i0_real_error4.4270e+07
Rg (reciprocal space) rg_reciprocal17.46
I(0) (reciprocal space) i0_reciprocal3610000000.0000
Solution quality estimate total_estimate0.8916
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.4
Skewness Skewness skewness0.339
Kurtosis Kurtosis kurtosis-0.291
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4277000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2a24a_
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_idd2a24b_
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_id2a24A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily20 — PAS domain
Domain ID domain_id2a24B01
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)