MolNFT v1 · #170315 · protein
14-3-3 sigma in complex with phosphorylated ATPase peptide
6Y3M · 14-3-3 protein sigma: “14-3-3 sigma in complex with phosphorylated ATPase peptide”. X-ray diffraction, 2 ligands (MG, CA), 1 pocket (best druggability 0.51). MolNFT v1 #170315 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6Y3M
- Type
- protein
- Length
- 240 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; ATPase peptide
- UniProt
- P31947
- Ligands
- MG, CA
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein sigma | protein | 236 | 80% helix, 0% strand | P31947 |
| P | ATPase peptide | 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.51 | 0.80 | 19 | empty |
Interfaces
1 interface between chains.
- A–P · 456 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
- Elsewhere: RCSB PDB 6Y3M · PDBe 6Y3M · UniProt P31947
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