2ilm

Factor Inhibiting HIF-1 Alpha D201A Mutant in Complex with FE(II), Alpha-Ketoglutarate and HIF-1 Alpha 35mer

Method: X-RAY DIFFRACTION Dmax: 70.3 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–349 Mutation:D201A Hypoxia-inducible factor 1 alpha × 2 (Q16665) FE2 FE (II) ION × 2 SO4 SULFATE ION × 4 BCT BICARBONATE ION × 2 AKG 2-OXOGLUTARIC ACID × 2 GOL GLYCEROL × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;1.6M AMMONIUM SULPHATE, 6% PEG400, 0.1M HEPES PH7.5 ARGON ATMOSPHERE, 14MG/ML PROTEIN WITH 1MM FE(II)SO4, 1MM ALPHA-KETOGLUTARATE, 1MM HIF-1ALPHA PEPTIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K, pH 7.50 Resolution 2.30 Å R-free 0.267

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 1–349; UniProt 1–349

Hypoxia-inducible factor 1 alpha

OrganismNot specified

UniProt Q16665

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain S; UniProt 786–826 Fragment:CTAD Hypoxia-inducible factor 1 alpha inhibitor × 2 (Q9NWT6) FE2 FE (II) ION × 2 SO4 SULFATE ION × 4 BCT BICARBONATE ION × 2 AKG 2-OXOGLUTARIC ACID × 2 GOL GLYCEROL × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;1.6M AMMONIUM SULPHATE, 6% PEG400, 0.1M HEPES PH7.5 ARGON ATMOSPHERE, 14MG/ML PROTEIN WITH 1MM FE(II)SO4, 1MM ALPHA-KETOGLUTARATE, 1MM HIF-1ALPHA PEPTIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K, pH 7.50 Resolution 2.30 Å R-free 0.267

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.

21 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HIF1A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain S; PDBConstruct 1–41; UniProt 786–826

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 2ilm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2ilm
Deposition date deposition_date2006-10-03
Structure title titleFactor Inhibiting HIF-1 Alpha D201A Mutant in Complex with FE(II), Alpha-Ketoglutarate and HIF-1 Alpha 35mer
Keywords keywords;FIH, HIF, DSBH, OXYGENASE, TRANSCRIPTION, HYPOXIA, INHIBITOR 2-OXOGLUTARATE, ASPARAGINYL HYDROXYLASE, TRANSCRIPTION REGULATOR, OXIDOREDUCTASE ;; TRANSCRIPTION REGULATOR, OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.48
Radius of gyration Rg (electron density) rg_electron20.30
Forward intensity I(0) i026377400.00
Molecular weight molecular_weight38723.0 kDa
Excluded volume excluded_volume48095 ų
Envelope volume envelope_volume58026 ų
Hydration-shell volume shell_volume23387 ų
Envelope diameter envelope_diameter71.6
Shell Rg shell_rg27.47
Envelope Rg envelope_rg20.74
Shape Rg shape_rg20.28
Total Rg total_rg21.31
Total atoms total_atoms2735
Residues n_residues347
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 dmax70.3
Rg (real space) rg_real21.36
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real2.6380e+07
I(0) uncertainty (real space) i0_real_error3.5180e+05
Rg (reciprocal space) rg_reciprocal21.38
I(0) (reciprocal space) i0_reciprocal26380000.0000
Solution quality estimate total_estimate0.8768
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.9
Skewness Skewness skewness0.236
Kurtosis Kurtosis kurtosis-0.242
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5864000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.811; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2ilma_
Class classb — All beta proteins
Fold Fold foldb.82 — Double-stranded beta-helix
Superfamily Superfamily superfamilyb.82.2 — Clavaminate synthase-like
Family Family familyb.82.2.6 — Hypoxia-inducible factor HIF ihhibitor (FIH1)

CATH v4.4 (2 domains)

Domain ID domain_id2ilmA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls
Domain ID domain_id2ilmA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily1010 — Clavaminate synthase-like

8. Citations (3)

9. Files and Curves (10)