3cbb

Crystal Structure of Hepatocyte Nuclear Factor 4alpha in complex with DNA: Diabetes Gene Product

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

Hepatocyte Nuclear Factor 4-alpha, DNA binding domain

Homo sapiens

UniProt P41235

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Homooligomer Protein 2 DNA 2 Hepatocyte Nuclear Factor 4-alpha promoter element DNA × 1 Hepatocyte Nuclear Factor 4-alpha promoter element DNA × 1 ZINC ION × 4 water × 4 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name HNF4A_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–78; UniProt 58–135 Author chain B; PDBConstruct 1–78; UniProt 58–135

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_id3cbb
Deposition date deposition_date2008-02-21
Structure title titleCrystal Structure of Hepatocyte Nuclear Factor 4alpha in complex with DNA: Diabetes Gene Product
Keywords keywordszinc finger, protein-DNA complex, diabetes, TRANSCRIPTION-DNA COMPLEX; TRANSCRIPTION/DNA
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.

3cbb__assembly_1__model_1

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

Download this curve (.dat)

3cbb__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.

3cbb__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)21.70 Å
Rg (electron density)21.26 Å
Total Rg21.95 Å
Atom count2089
Residues196
Excluded volume34164 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3cbb__assembly_1__model_1 tetrameric (4) 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) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3cbba_
Class classg — Small proteins
Fold Fold foldg.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamilyg.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family familyg.39.1.2 — Nuclear receptor
Domain ID domain_idd3cbbb_
Class classg — Small proteins
Fold Fold foldg.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamilyg.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family familyg.39.1.2 — Nuclear receptor

CATH v4.4 (2 domains)

Domain ID domain_id3cbbA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily10 — Erythroid Transcription Factor GATA-1, subunit A
Domain ID domain_id3cbbB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily10 — Erythroid Transcription Factor GATA-1, subunit A
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7. Citations (2)