1yci

Factor inhibiting HIF-1 alpha in complex with N-(carboxycarbonyl)-D-phenylalanine

Method: X-RAY DIFFRACTION Dmax: 71.2 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–349 Not recorded FE2 FE (II) ION × 2 SO4 SULFATE ION × 6 NDF N-(CARBOXYCARBONYL)-D-PHENYLALANINE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;1.2M AMMONIUM SULPHATE, 4% PEG400, 0.1M HEPES PH7.5 ARGON ATMOSPHERE, 28MG/ML PROTEIN WITH 1MM FE(II), 10MM N-(CARBOXYCARBONYL)-D-PHENYLALANINE, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.70 Å R-free 0.244

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 1yci

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1yci
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1yci
Deposition date deposition_date2004-12-22
Structure title titleFactor inhibiting HIF-1 alpha in complex with N-(carboxycarbonyl)-D-phenylalanine
Keywords keywords;FIH, HIF, DSBH, OXYGENASE, TRANSCRIPTION, HYPOXIA, INHIBITOR 2-OXOGLUTARATE, ASPARAGINYL HYDROXYLASE, HYDROXYLASE N-(CARBOXYCARBONYL)-D-PHENYLALANINE, NOFD, NDF, 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_guinier21.84
Radius of gyration Rg (electron density) rg_electron20.60
Forward intensity I(0) i027037700.00
Molecular weight molecular_weight39173.0 kDa
Excluded volume excluded_volume48641 ų
Envelope volume envelope_volume58625 ų
Hydration-shell volume shell_volume23437 ų
Envelope diameter envelope_diameter72.2
Shell Rg shell_rg27.68
Envelope Rg envelope_rg20.94
Shape Rg shape_rg20.56
Total Rg total_rg21.62
Total atoms total_atoms2765
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 dmax71.2
Rg (real space) rg_real21.72
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.7040e+07
I(0) uncertainty (real space) i0_real_error3.7210e+05
Rg (reciprocal space) rg_reciprocal21.75
I(0) (reciprocal space) i0_reciprocal27040000.0000
Solution quality estimate total_estimate0.8808
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.269
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha5374000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.967

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_idd1ycia_
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_id1yciA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls
Domain ID domain_id1yciA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily1010 — Clavaminate synthase-like

8. Citations (2)

9. Files and Curves (10)