Research workbench
Crystal structure of SMAD2 MH2 domain bound to the smad-binding domain of sara
Analyse Crystal structure of SMAD2 MH2 domain bound to the smad-binding domain of sara in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DEV
- Type
- protein
- Length
- 466 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q15796, O95405
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 194 | — | Q15796 |
| B | — | protein | 41 | — | O95405 |
| C | — | protein | 192 | — | Q15796 |
| D | — | protein | 39 | — | O95405 |
Compared structures
- 1DEV · Crystal structure of SMAD2 MH2 domain bound to the smad-binding domain of sara · the same entry in another collection · chain D against D, TM-score 1.00
- Q15796 · AlphaFold monomer V2.0 prediction for mothers against decapentaplegic homolog 2 (Q15796) · a predicted model of the same protein · chain A against A, TM-score 0.97
- O95405 · AlphaFold monomer V2.0 prediction for zinc finger fyve domain- containing protein 9… · a predicted model of the same protein · chain D against A, TM-score 0.41
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q15796
- Every structure of UniProt O95405
- Elsewhere: RCSB PDB 1DEV · PDBe 1DEV · UniProt Q15796 · UniProt O95405
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