MolNFT v1 · #184460 · protein
Ternary complex of 14-3-3 sigma, amot-P130 phosphopeptide, and WQ178
7OQW · 14-3-3 protein sigma: “Ternary complex of 14-3-3 sigma, amot-P130 phosphopeptide, and WQ178”. X-ray diffraction, 2 ligands (0B7, MG), 1 pocket (best druggability 0.40). MolNFT v1 #184460 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7OQW
- Type
- protein
- Length
- 229 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; Amot-P130 phosphopeptide (PS175)
- UniProt
- P31947, Q4VCS5
- Ligands
- 0B7, MG
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein sigma | protein | 224 | 84% helix, 0% strand | P31947 |
| P | Amot-P130 phosphopeptide (PS175) | protein | 5 | 0% helix, 0% strand | Q4VCS5 |
Ligands and binding sites
- 0B7 · ~{N}-[(5-carbamimidoyl-3-phenyl-thiophen-2-yl)methyl]-1~{H}-indole-6-carboxamide · ligand · 2 copies · chains A
- MG · Magnesium ion · metal · 2 copies · 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 | 114 | 0.40 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–P · 518 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation, phosphorylation).
Compared structures
- 7OQW · Ternary complex of 14-3-3 sigma, Amot-p130 phosphopeptide, and WQ178 · the same entry in another collection · chain A against A, TM-score 1.00
- P31947 · AlphaFold monomer V2.0 prediction for 14-3-3 protein sigma (P31947) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q4VCS5 · AlphaFold monomer V2.0 prediction for angiomotin (Q4VCS5) · a predicted model of the same protein · chain P against A, TM-score 0.62
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 Q4VCS5
- Elsewhere: RCSB PDB 7OQW · PDBe 7OQW · UniProt P31947 · UniProt Q4VCS5
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