Research workbench
Solution NMR structure of the P300 TAZ2:ETAD1 complex
Analyse Solution NMR structure of the P300 TAZ2:ETAD1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MH0
- Type
- protein
- Length
- 131 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription factor E2-alpha; Histone acetyltransferase P300
- EC
- 2.3.1.48
- UniProt
- P15923, Q09472
Structure
solution nmr · 2 distinct chains · 55% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription factor E2-alpha | protein | 39 | 36% helix, 0% strand | P15923 |
| B | Histone acetyltransferase P300 (EC 2.3.1.48) | protein | 92 | 63% helix, 0% strand | Q09472 |
Interfaces
1 interface between chains.
- A–B · 817 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2MH0 · Solution NMR structure of the p300 Taz2:ETAD1 complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q09472 · AlphaFold monomer V2.0 prediction for histone acetyltransferase P300 (Q09472) · a predicted model of the same protein · chain B against A, TM-score 0.81
- P15923 · AlphaFold monomer V2.0 prediction for transcription factor E2-alpha (P15923) · a predicted model of the same protein · chain A against A, TM-score 0.43
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 P15923
- Every structure of UniProt Q09472
- Elsewhere: RCSB PDB 2MH0 · PDBe 2MH0 · UniProt P15923 · UniProt Q09472
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