Research workbench
Solution structure of the complex between BCL-xl and the P53 core domain determined with pre restraints
Analyse Solution structure of the complex between BCL-xl and the P53 core domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MEJ
- Type
- protein
- Length
- 339 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BCL-2-like protein 1; Cellular tumor antigen P53
- UniProt
- Q07817, P04637
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.82
Structure
solution nmr · 2 distinct chains · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BCL-2-like protein 1 | protein | 144 | 72% helix, 0% strand | Q07817 |
| B | Cellular tumor antigen P53 | protein | 195 | 9% helix, 37% strand | P04637 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 237 | 0.82 | 0.94 | 44 | empty |
| 2 | 138 | 0.76 | 0.94 | 28 | empty |
| 3 | 124 | 0.44 | 0.77 | 26 | empty |
| 4 | 88 | 0.37 | 0.76 | 16 | empty |
| 5 | 64 | 0.35 | 0.78 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1096 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 2MEJ · Solution Structure of the Complex Between BCL-xL and the p53 Core Domain determined with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q07817 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 1 (Q07817) · a predicted model of the same protein · chain A against A, TM-score 0.73
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 Q07817
- Every structure of UniProt P04637
- Elsewhere: RCSB PDB 2MEJ · PDBe 2MEJ · UniProt Q07817 · UniProt P04637
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