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1tqe

Mechanism of recruitment of class II histone deacetylases by myocyte enhancer factor-2

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

Myocyte-specific enhancer factor 2B

Homo sapiens

UniProt Q02080

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 3 DNA 2 MEF2 binding site of nur77 promoter × 1 MEF2 binding site of nur77 promoter × 1 Histone deacetylase 9 × 1 （Q99N13） Consistent with all polymers
2 Protein–DNA Heteromer Protein 3 DNA 2 MEF2 binding site of nur77 promoter × 1 MEF2 binding site of nur77 promoter × 1 Histone deacetylase 9 × 1 （Q99N13） Consistent with all polymers

Other States of the Same Protein in the Database

Monomer

None

Homodimer
6c9l 6c9l 6c9l

3 assemblies

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
1n6j 1tqe 1tqe 6byy 6byy 6bz1 6bz1 6wc2 6wc2 6wc2 6wc5 6wc5

12 assemblies

View Construct and Data Evidence
UniProt name MEF2B_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain P； PDBConstruct 1–93； UniProt 1–93 Author chain Q； PDBConstruct 1–93； UniProt 1–93 Author chain R； PDBConstruct 1–93； UniProt 1–93 Author chain S； PDBConstruct 1–93； UniProt 1–93

Histone deacetylase 9

Mus musculus

UniProt Q99N13

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 3 DNA 2 MEF2 binding site of nur77 promoter × 1 MEF2 binding site of nur77 promoter × 1 Myocyte-specific enhancer factor 2B × 2 （Q02080） Consistent with all polymers
2 Protein–DNA Heteromer Protein 3 DNA 2 MEF2 binding site of nur77 promoter × 1 MEF2 binding site of nur77 promoter × 1 Myocyte-specific enhancer factor 2B × 2 （Q02080） Consistent with all polymers

Other States of the Same Protein in the Database

Monomer

None

Homodimer

None

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
1tqe 1tqe

2 assemblies

View Construct and Data Evidence
UniProt name HDAC9_MOUSE
Isoform —
PDB entities 4
Chains and sequence ranges Author chain X； PDBConstruct 6–26； UniProt 138–158 Author chain Y； PDBConstruct 6–26； UniProt 138–158

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_id1tqe
Deposition date deposition_date2004-06-17
Structure title titleMechanism of recruitment of class II histone deacetylases by myocyte enhancer factor-2
Keywords keywordsMEF2, HDAC, co-repressor, transcription, TRANSCRIPTION-PROTEIN BINDING-DNA COMPLEX; TRANSCRIPTION/PROTEIN BINDING/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.

1tqe__assembly_1__model_1

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

Download this curve (.dat)

1tqe__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.

1tqe__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）20.79 Å
Rg (electron density)19.43 Å
Total Rg20.32 Å
Atom count2365
Residues237
Excluded volume40206 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1tqe__assembly_1__model_1 pentameric （5） Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1tqe__assembly_2__model_1 pentameric （5） 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 (4)

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1tqep_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.88 — SRF-like
Superfamily Superfamily superfamilyd.88.1 — SRF-like
Family Family familyd.88.1.1 — SRF-like
Domain ID domain_idd1tqeq_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.88 — SRF-like
Superfamily Superfamily superfamilyd.88.1 — SRF-like
Family Family familyd.88.1.1 — SRF-like
Domain ID domain_idd1tqer_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.88 — SRF-like
Superfamily Superfamily superfamilyd.88.1 — SRF-like
Family Family familyd.88.1.1 — SRF-like
Domain ID domain_idd1tqes_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.88 — SRF-like
Superfamily Superfamily superfamilyd.88.1 — SRF-like
Family Family familyd.88.1.1 — SRF-like

CATH v4.4 (4 domains)

Domain ID domain_id1tqeP01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1810 — SRF-like
Homologous superfamily homologous superfamily10 — Transcription factor, MADS-box
Domain ID domain_id1tqeQ01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1810 — SRF-like
Homologous superfamily homologous superfamily10 — Transcription factor, MADS-box
Domain ID domain_id1tqeR01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1810 — SRF-like
Homologous superfamily homologous superfamily10 — Transcription factor, MADS-box
Domain ID domain_id1tqeS01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1810 — SRF-like
Homologous superfamily homologous superfamily10 — Transcription factor, MADS-box
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7. Citations (1)