9fsn

FIH in complex with Enarodustat crystal structure at 2.2A

Method: X-RAY DIFFRACTION Dmax: 71.1 Å Quality: REASONABLE

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

Hypoxia-inducible factor 1-alpha inhibitor

Homo sapiens

UniProt Q9NWT6

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–349 Not recorded MN MANGANESE (II) ION × 2 A1IF7 Enarodustat × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;290 K;Morpheus 1, well C1, 0.09 M NPS, 0.1 M Buffer System 1 pH 6.5, 30 % Precipitant Mix 1 Resolution 2.20 Å R-free 0.208

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.

60 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HIF1N_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–350; UniProt 1–349

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 9fsn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fsn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fsn
Deposition date deposition_date2024-06-21
最后修订 last_revision2025-01-29
Structure title titleFIH in complex with Enarodustat crystal structure at 2.2A
Keywords keywordsFIH, oxygenase, Complex, inhibitor, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.72
Radius of gyration Rg (electron density) rg_electron20.71
Forward intensity I(0) i049962700.00
Molecular weight molecular_weight36856.0 kDa
Excluded volume excluded_volume35778 ų
Envelope volume envelope_volume59882 ų
Hydration-shell volume shell_volume23769 ų
Envelope diameter envelope_diameter73.5
Shell Rg shell_rg27.83
Envelope Rg envelope_rg21.14
Shape Rg shape_rg20.67
Total Rg total_rg21.48
Total atoms total_atoms2796
Residues n_residues336
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 dmax71.1
Rg (real space) rg_real21.62
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real4.9960e+07
I(0) uncertainty (real space) i0_real_error5.6510e+05
Rg (reciprocal space) rg_reciprocal21.64
I(0) (reciprocal space) i0_reciprocal49960000.0000
Solution quality estimate total_estimate0.6988
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.0
Skewness Skewness skewness0.264
Kurtosis Kurtosis kurtosis-0.263
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8202000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 1.000; Sysdev: 0.207; Positv: 1.000; Valcen: 1.000; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)