3hqr

PHD2:Mn:NOG:HIF1-alpha substrate complex

Method: X-RAY DIFFRACTION Dmax: 58.4 Å Quality: REASONABLE

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 181–426 Fragment:PHD2 catalytic domain, residues 181-426 Mutation:R398A Hypoxia-inducible factor 1 alpha × 1 (Q16665) MN MANGANESE (II) ION × 1 OGA N-OXALYLGLYCINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:hanging drop;pH 7.5;298 K;20% PEG 3350, 200mM MgCl2, pH 7.5, hanging drop, temperature 298K Resolution 2.00 Å R-free 0.248

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 1–246; UniProt 181–426

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain S; UniProt 558–574 Fragment:C-terminal degradation domain, residues 558-574 Egl nine homolog 1 × 1 (Q9GZT9) MN MANGANESE (II) ION × 1 OGA N-OXALYLGLYCINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:hanging drop;pH 7.5;298 K;20% PEG 3350, 200mM MgCl2, pH 7.5, hanging drop, temperature 298K Resolution 2.00 Å R-free 0.248

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 1–17; UniProt 558–574

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 3hqr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3hqr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3hqr
Deposition date deposition_date2009-06-08
Structure title titlePHD2:Mn:NOG:HIF1-alpha substrate complex
Keywords keywords;double stranded beta-helix, Alternative splicing, Congenital erythrocytosis, Dioxygenase, Disease mutation, Iron, Metal-binding, Oxidoreductase, Vitamin C, Zinc, Zinc-finger, Activator, Cytoplasm, DNA-binding, Hydroxylation, Isopeptide bond, Nucleus, Phosphoprotein, Polymorphism, S-nitrosylation, Transcription, Transcription regulation, Ubl conjugation, OXIDOREDUCTASE-TRANSCRIPTION COMPLEX ;; OXIDOREDUCTASE/TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.55
Radius of gyration Rg (electron density) rg_electron16.45
Forward intensity I(0) i013419600.00
Molecular weight molecular_weight27220.0 kDa
Excluded volume excluded_volume33928 ų
Envelope volume envelope_volume36703 ų
Hydration-shell volume shell_volume17944 ų
Envelope diameter envelope_diameter61.6
Shell Rg shell_rg23.33
Envelope Rg envelope_rg17.19
Shape Rg shape_rg16.44
Total Rg total_rg17.51
Total atoms total_atoms1910
Residues n_residues242
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 dmax58.4
Rg (real space) rg_real17.42
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real1.3420e+07
I(0) uncertainty (real space) i0_real_error1.5210e+05
Rg (reciprocal space) rg_reciprocal17.44
I(0) (reciprocal space) i0_reciprocal13420000.0000
Solution quality estimate total_estimate0.6401
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.140
Kurtosis Kurtosis kurtosis-0.292
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4382000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.744; Stabil: 0.999; Sysdev: 0.363; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3hqrA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily620 — q2cbj1_9rhob like domain

8. Citations (2)

9. Files and Curves (10)