Research workbench
Cryo-EM structure of P300-P53 protein complex
Analyse Cryo-EM structure of P300-P53 protein complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XZC
- Type
- protein
- Length
- 1,547 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase P300; Cellular tumor antigen P53
- EC
- 2.3.1.48
- UniProt
- Q09472, P04637
- Pockets
- 1 · best druggability 0.28
Structure
electron microscopy · 2 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase P300 (EC 2.3.1.48) | protein | 619 | 0% helix, 0% strand | Q09472 |
| B, C, D, E | Cellular tumor antigen P53 | protein | 232 | 0% helix, 0% strand | P04637 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.28 | 0.73 | 17 | empty |
Interfaces
5 interfaces between chains.
- B–D · 170 Ų buried · 0 hydrogen bonds · protein-protein
- C–E · 170 Ų buried · 0 hydrogen bonds · protein-protein
- D–E · 97 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 64 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 53 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 Q09472
- Every structure of UniProt P04637
- Elsewhere: RCSB PDB 5XZC · PDBe 5XZC · UniProt Q09472 · UniProt P04637
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