7q5v

HIF PROLYL HYDROXYLASE 2 (PHD2/EGLN1) IN COMPLEX WITH N-OXALYLGLYCINE (NOG) AND HIF-2 ALPHA CODD (523-542)

Method: X-RAY DIFFRACTION Dmax: 57.5 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) MN MANGANESE (II) ION × 1 OGA N-OXALYLGLYCINE × 1 PEG DI(HYDROXYETHYL)ETHER × 3 GOL GLYCEROL × 1 FMT FORMIC ACID × 3 CL CHLORIDE ION × 1 MG MAGNESIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;Sample: 1.0 mM PHD2, 1.2 mM MnCl2, 2.0 mM NOG, 2 mM 3C, 2-4 mM HIF-2alpha-CODD; Reservoir: 0.31 M Magnesium formate (range: 0.25-0.39 M), 16.6% w/v polyethylene glycol 3350 (range: 18-22%); Sitting drop (200 nl): protein-to-well ratio, 1:1; Cryo-protectant: 15% v/v dilution of reservoir with glycerol Resolution 1.17 Å R-free 0.179

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

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 523–542 Not recorded Egl nine homolog 1 × 1 (Q9GZT9) MN MANGANESE (II) ION × 1 OGA N-OXALYLGLYCINE × 1 PEG DI(HYDROXYETHYL)ETHER × 3 GOL GLYCEROL × 1 FMT FORMIC ACID × 3 CL CHLORIDE ION × 1 MG MAGNESIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;Sample: 1.0 mM PHD2, 1.2 mM MnCl2, 2.0 mM NOG, 2 mM 3C, 2-4 mM HIF-2alpha-CODD; Reservoir: 0.31 M Magnesium formate (range: 0.25-0.39 M), 16.6% w/v polyethylene glycol 3350 (range: 18-22%); Sitting drop (200 nl): protein-to-well ratio, 1:1; Cryo-protectant: 15% v/v dilution of reservoir with glycerol Resolution 1.17 Å R-free 0.179

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 7q5v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7q5v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7q5v
Deposition date deposition_date2021-11-04
Structure title titleHIF PROLYL HYDROXYLASE 2 (PHD2/EGLN1) IN COMPLEX WITH N-OXALYLGLYCINE (NOG) AND HIF-2 ALPHA CODD (523-542)
Keywords keywordsPHD2, HIF-2Alpha, Complex, OXIDOREDUCTASE, Hypoxia; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.08
Radius of gyration Rg (electron density) rg_electron16.92
Forward intensity I(0) i014321400.00
Molecular weight molecular_weight27997.0 kDa
Excluded volume excluded_volume34827 ų
Envelope volume envelope_volume39357 ų
Hydration-shell volume shell_volume18812 ų
Envelope diameter envelope_diameter58.2
Shell Rg shell_rg23.77
Envelope Rg envelope_rg17.34
Shape Rg shape_rg16.91
Total Rg total_rg17.98
Total atoms total_atoms3853
Residues n_residues243
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 dmax57.5
Rg (real space) rg_real17.91
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real1.4320e+07
I(0) uncertainty (real space) i0_real_error1.7060e+05
Rg (reciprocal space) rg_reciprocal17.93
I(0) (reciprocal space) i0_reciprocal14320000.0000
Solution quality estimate total_estimate0.8844
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.077
Kurtosis Kurtosis kurtosis-0.438
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4784000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.839; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)