8q6e

Aerobic crystal structure of HIF prolyl hydroxylase 2 (PHD2 181-407) in complex with Fe(III), 2-oxoglutarate (2OG) and HIF2alpha-CODD peptide

Method: X-RAY DIFFRACTION Dmax: 53.5 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 Endothelial PAS domain-containing protein 1 × 1 (Q99814) MG MAGNESIUM ION × 3 CL CHLORIDE ION × 2 FE FE (III) ION × 1 AKG 2-OXOGLUTARIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;(10-35%) PEG 4K, 0.2 M ammonium acetate , 0.1 M sodium ammonium acetate trihydrate pH (4.1-5.6) Resolution 1.37 Å R-free 0.205

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 7–233; UniProt 181–407

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 B; UniProt 523–542 Not recorded Egl nine homolog 1 × 1 (Q9GZT9) MG MAGNESIUM ION × 3 CL CHLORIDE ION × 2 FE FE (III) ION × 1 AKG 2-OXOGLUTARIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;(10-35%) PEG 4K, 0.2 M ammonium acetate , 0.1 M sodium ammonium acetate trihydrate pH (4.1-5.6) Resolution 1.37 Å R-free 0.205

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 1–20; UniProt 523–542

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 8q6e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8q6e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8q6e
Deposition date deposition_date2023-08-11
最后修订 last_revision2024-08-21
Structure title titleAerobic crystal structure of HIF prolyl hydroxylase 2 (PHD2 181-407) in complex with Fe(III), 2-oxoglutarate (2OG) and HIF2alpha-CODD peptide
Keywords keywords2OG oxygenases, oxygen sensor, jelly-roll, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.71
Radius of gyration Rg (electron density) rg_electron16.50
Forward intensity I(0) i012742400.00
Molecular weight molecular_weight26166.0 kDa
Excluded volume excluded_volume32486 ų
Envelope volume envelope_volume36308 ų
Hydration-shell volume shell_volume17900 ų
Envelope diameter envelope_diameter54.7
Shell Rg shell_rg23.19
Envelope Rg envelope_rg16.88
Shape Rg shape_rg16.50
Total Rg total_rg17.53
Total atoms total_atoms3550
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 dmax53.5
Rg (real space) rg_real17.55
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real1.2740e+07
I(0) uncertainty (real space) i0_real_error1.3840e+05
Rg (reciprocal space) rg_reciprocal17.57
I(0) (reciprocal space) i0_reciprocal12740000.0000
Solution quality estimate total_estimate0.8232
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.061
Kurtosis Kurtosis kurtosis-0.457
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3519000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.906; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)