Research workbench
Extended sid of MAD1 bound to the PAH2 domain of MSIN3B
Analyse Extended sid of MAD1 bound to the PAH2 domain of MSIN3B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PD7
- Type
- protein
- Length
- 109 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SIN3B protein; MAD1
- UniProt
- Q62141, Q05195
Structure
solution nmr · 2 distinct chains · 64% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SIN3B protein | protein | 85 | 61% helix, 0% strand | Q62141 |
| B | MAD1 | protein | 24 | 75% helix, 0% strand | Q05195 |
Interfaces
1 interface between chains.
- A–B · 955 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1PD7 · Extended SID of Mad1 bound to the PAH2 domain of mSin3B · the same entry in another collection · chain A against A, TM-score 1.00
- Q62141 · AlphaFold monomer V2.0 prediction for paired amphipathic helix protein SIN3B (Q62141) · a predicted model of the same protein · chain A against A, TM-score 0.77
- Q05195 · AlphaFold monomer V2.0 prediction for max dimerization protein 1 (Q05195) · a predicted model of the same protein · chain B against A, TM-score 0.56
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 Q62141
- Every structure of UniProt Q05195
- Elsewhere: RCSB PDB 1PD7 · PDBe 1PD7 · UniProt Q62141 · UniProt Q05195
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