3hqr

PHD2:Mn:NOG:HIF1-alpha substrate complex

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Egl nine homolog 1

Homo sapiens

UniProt Q9GZT9

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Hypoxia-inducible factor 1 alpha × 1 (Q16665) MANGANESE (II) ION × 1 N-OXALYLGLYCINE × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Egl nine homolog 1 × 1 (Q9GZT9) MANGANESE (II) ION × 1 N-OXALYLGLYCINE × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

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.

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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
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

3hqr__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3hqr__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

3hqr__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)17.55 Å
Rg (electron density)16.45 Å
Total Rg17.51 Å
Atom count1910
Residues242
Excluded volume33928 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3hqr__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

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6. 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
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7. Citations (2)