1mk2

SMAD3 SBD complex

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

SMAD 3

Homo sapiens

UniProt P84022

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Madh-interacting protein × 2 (O95405) ACETIC ACID × 8 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 2 Madh-interacting protein × 1 (O95405) ACETIC ACID × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name SMAD3_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–206; UniProt 220–425

Madh-interacting protein

Homo sapiens

UniProt O95405

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 SMAD 3 × 2 (P84022) ACETIC ACID × 8 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 2 SMAD 3 × 1 (P84022) ACETIC ACID × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ZFYV9_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–38; UniProt 773–810

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_id1mk2
Deposition date deposition_date2002-08-28
Structure title titleSMAD3 SBD complex
Keywords keywordsSMAD3, SBD, SARA, TRANSCRIPTION; 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.

1mk2__assembly_1__model_1

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

Download this curve (.dat)

1mk2__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.

1mk2__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)24.72 Å
Rg (electron density)23.77 Å
Total Rg24.63 Å
Atom count3696
Residues470
Excluded volume65341 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1mk2__assembly_1__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1mk2__assembly_2__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 (3)

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1mk2a_
Class classb — All beta proteins
Fold Fold foldb.26 — SMAD/FHA domain
Superfamily Superfamily superfamilyb.26.1 — SMAD/FHA domain
Family Family familyb.26.1.1 — SMAD domain
Domain ID domain_idd1mk2b_
Class classj — Peptides
Fold Fold foldj.64 — Smad-binding domain of Sara
Superfamily Superfamily superfamilyj.64.1 — Smad-binding domain of Sara
Family Family familyj.64.1.1 — Smad-binding domain of Sara

CATH v4.4 (1 domains)

Domain ID domain_id1mk2A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily10 —
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7. Citations (1)