2cgo

FACTOR INHIBITING HIF-1 ALPHA with fumarate

Method: X-RAY DIFFRACTION Dmax: 70.6 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–349 Not recorded FE FE (III) ION × 1 FUM FUMARIC ACID × 1 SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;1.25M AMMONIUM SULFATE, 100MM HEPES PH7.5, 6% PEG400, 1MM IRON (II) SULFATE, 20MM FUMARIC ACID, pH 7.50 Resolution 2.30 Å R-free 0.237

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

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 2cgo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2cgo
Deposition date deposition_date2006-03-09
Structure title titleFACTOR INHIBITING HIF-1 ALPHA with fumarate
Keywords keywords;OXIDOREDUCTASE, 2-OXOGLUTARATE, ACETYLATION, ACTIVATOR, ALTERNATIVE SPLICING, ASPARAGINYL HYDROXYLASE, DNA-BINDING, DSBH, FI, HIF, HYDROXYLATION, HYPOXIA, NUCLEAR PROTEIN, OXYGENASE, PHOSPHORYLATION, POLYMORPHISM, S-NITROSYLATION, TRANSCRIPTION, TRANSCRIPTION ACTIVATOR/INHIBITOR, TRANSCRIPTION REGULATION, DIOXYGENASE, IRON, METAL-BINDING ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.88
Radius of gyration Rg (electron density) rg_electron20.67
Forward intensity I(0) i027966400.00
Molecular weight molecular_weight39811.0 kDa
Excluded volume excluded_volume49478 ų
Envelope volume envelope_volume60249 ų
Hydration-shell volume shell_volume23818 ų
Envelope diameter envelope_diameter72.6
Shell Rg shell_rg27.94
Envelope Rg envelope_rg21.18
Shape Rg shape_rg20.64
Total Rg total_rg21.74
Total atoms total_atoms2806
Residues n_residues339
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 dmax70.6
Rg (real space) rg_real21.76
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real2.7970e+07
I(0) uncertainty (real space) i0_real_error3.3100e+05
Rg (reciprocal space) rg_reciprocal21.78
I(0) (reciprocal space) i0_reciprocal27970000.0000
Solution quality estimate total_estimate0.8833
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4
Skewness Skewness skewness0.231
Kurtosis Kurtosis kurtosis-0.283
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5611000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.846; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2cgoa_
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_id2cgoA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls
Domain ID domain_id2cgoA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily1010 — Clavaminate synthase-like

8. Citations (1)

9. Files and Curves (10)