5zok

X-ray diffraction
2.85Å resolution

Crystal structure of human SMAD1-MAN1 complex.

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for receptor-regulated SMAD recognition by MAN1.
OpenAccess logo Nucleic Acids Res 46 12139-12153 (2018)
PMID: 30321401

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-172412 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mothers against decapentaplegic homolog 1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 209 amino acids
Theoretical weight: 23.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15797 (Residues: 259-462; Coverage: 44%)
Gene names: BSP1, MADH1, MADR1, SMAD1
Sequence domains: MH2 domain
Structure domains: Tumour Suppressor Smad4
Inner nuclear membrane protein Man1 Chains: B, D
Molecule details ›
Chains: B, D
Length: 132 amino acids
Theoretical weight: 14.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y2U8 (Residues: 762-890; Coverage: 14%)
Gene names: LEMD3, MAN1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P4132
Unit cell:
a: 187.05Å b: 187.05Å c: 187.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.215 0.255
Expression system: Escherichia coli