Research workbench
Solution structure of the MSIN3A PAH1-SAP25 sid complex
Analyse Solution structure of the MSIN3A PAH1-SAP25 sid complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RMS
- Type
- protein
- Length
- 132 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Paired amphipathic helix protein SIN3A; MSIN3A-binding protein
- UniProt
- Q60520, Q1EHW4
Structure
solution nmr · 2 distinct chains · 48% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Paired amphipathic helix protein SIN3A | protein | 71 | 72% helix, 0% strand | Q60520 |
| B | MSIN3A-binding protein | protein | 61 | 21% helix, 0% strand | Q1EHW4 |
Interfaces
1 interface between chains.
- A–B · 760 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2RMS · Solution structure of the mSin3A PAH1-SAP25 SID complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q60520 · AlphaFold monomer V2.0 prediction for paired amphipathic helix protein SIN3A (Q60520) · a predicted model of the same protein · chain A against A, TM-score 0.85
- Q1EHW4 · AlphaFold monomer V2.0 prediction for histone deacetylase complex subunit SAP25 (Q1EHW4) · a predicted model of the same protein · chain B against A, TM-score 0.32
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 Q60520
- Every structure of UniProt Q1EHW4
- Elsewhere: RCSB PDB 2RMS · PDBe 2RMS · UniProt Q60520 · UniProt Q1EHW4
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