MolNFT v1 · #170465 · protein
14-3-3 sigma in complex with phosphorylated CASPASE{PS164} peptide
6Y8D · 14-3-3 protein sigma: “14-3-3 sigma in complex with phosphorylated CASPASE{PS164} peptide”. X-ray diffraction, 2 ligands (MG, CL), 1 pocket (best druggability 0.43). MolNFT v1 #170465 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6Y8D
- Type
- protein
- Length
- 238 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; Val-glu-his-sep-leu-asp-asn-lys
- UniProt
- P31947
- Ligands
- MG, CL
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein sigma | protein | 234 | 79% helix, 0% strand | P31947 |
| B | Val-glu-his-sep-leu-asp-asn-lys | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
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 | 122 | 0.43 | 0.77 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 385 Ų buried · 11 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
- Elsewhere: RCSB PDB 6Y8D · PDBe 6Y8D · UniProt P31947
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