8ruz

Anaerobic HIF prolyl-hydroxylase-2 (PHD2) T387S variant bound to acetate (ACT) and Hypoxia-inducible Factor-2alpha (HIF-2alpha)

Method: X-RAY DIFFRACTION Dmax: 55.4 Å Quality: GOOD

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

Egl nine homolog 1

Homo sapiens

UniProt Q9GZT9

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 181–407 Not recorded Hypoxia-inducible Factor-2alpha × 1 (Q99814) ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;297 K;(10-35%) PEG 4K, 0.2 M ammonium acetate and 0.1 M sodium ammonium acetate trihydrate pH (4.1-5.6). Resolution 1.82 Å R-free 0.314

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.

63 other PDB entries and 84 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EGLN1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–227; UniProt 181–407

Hypoxia-inducible Factor-2alpha

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 B; UniProt 524–542 Not recorded Egl nine homolog 1 × 1 (Q9GZT9) ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;297 K;(10-35%) PEG 4K, 0.2 M ammonium acetate and 0.1 M sodium ammonium acetate trihydrate pH (4.1-5.6). Resolution 1.82 Å R-free 0.314

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–19; UniProt 524–542

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 8ruz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ruz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ruz
Deposition date deposition_date2024-01-31
最后修订 last_revision2025-02-12
Structure title titleAnaerobic HIF prolyl-hydroxylase-2 (PHD2) T387S variant bound to acetate (ACT) and Hypoxia-inducible Factor-2alpha (HIF-2alpha)
Keywords keywords2OG oxygenase, Oxygen sensing, Prolyl Hydroxylase, substrate complex, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.73
Radius of gyration Rg (electron density) rg_electron16.56
Forward intensity I(0) i012271300.00
Molecular weight molecular_weight26108.0 kDa
Excluded volume excluded_volume32589 ų
Envelope volume envelope_volume36636 ų
Hydration-shell volume shell_volume17987 ų
Envelope diameter envelope_diameter54.3
Shell Rg shell_rg23.27
Envelope Rg envelope_rg16.94
Shape Rg shape_rg16.56
Total Rg total_rg17.60
Total atoms total_atoms3583
Residues n_residues238
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 dmax55.4
Rg (real space) rg_real17.57
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real1.2270e+07
I(0) uncertainty (real space) i0_real_error1.3520e+05
Rg (reciprocal space) rg_reciprocal17.59
I(0) (reciprocal space) i0_reciprocal12270000.0000
Solution quality estimate total_estimate0.8900
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.052
Kurtosis Kurtosis kurtosis-0.462
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3512000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)