Research workbench
Binary complex of 14-3-3 sigma and P53 PT387-peptide
Analyse Binary complex of 14-3-3 sigma and P53 PT387-peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LW1
- Type
- protein
- Length
- 242 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; Peptide of cellular tumor antigen P53
- UniProt
- P31947, P04637
- Ligands
- MG, CL
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein sigma | protein | 235 | 80% helix, 0% strand | P31947 |
| P | Peptide of cellular tumor antigen P53 | protein | 7 | 0% helix, 0% strand | P04637 |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 86 | 0.37 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–P · 604 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation, phosphorylation).
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 P31947
- Every structure of UniProt P04637
- Elsewhere: RCSB PDB 3LW1 · PDBe 3LW1 · UniProt P31947 · UniProt P04637
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