Research workbench
Solution structure of the CITED2 transactivation domain in complex with the P300 CH1 domain
Analyse Solution structure of the CITED2 transactivation domain in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P4Q
- Type
- protein
- Length
- 153 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CBP/P300-interacting transactivator 2; E1A-associated protein P300
- EC
- 2.3.1.48
- UniProt
- Q99967, Q09472
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.39
Structure
solution nmr · 2 distinct chains · 44% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CBP/P300-interacting transactivator 2 | protein | 52 | 23% helix, 0% strand | Q99967 |
| B | E1A-associated protein P300 (EC 2.3.1.48) | protein | 101 | 55% helix, 0% strand | Q09472 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.39 | 0.78 | 20 | empty |
| 2 | 56 | 0.30 | 0.76 | 16 | empty |
| 3 | 56 | 0.29 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2183 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1P4Q · Solution structure of the CITED2 transactivation domain in complex with the p300 CH1… · 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 0.73
- Q99967 · AlphaFold monomer V2.0 prediction for CBP/P300-interacting transactivator 2 (Q99967) · a predicted model of the same protein · chain A against A, TM-score 0.59
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 Q99967
- Every structure of UniProt Q09472
- Elsewhere: RCSB PDB 1P4Q · PDBe 1P4Q · UniProt Q99967 · UniProt Q09472
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