MolNFT v1 · #151403 · protein
Ternary complex of estrogen receptor alpha peptide and 14-3-3 sigma C42 mutant bound to disulfide fragment ppi stabilizer 2
6HMT · 14-3-3 protein sigma: “Ternary complex of estrogen receptor alpha peptide and 14-3-3 sigma C42 mutant bound to disulfide fragment…”. X-ray diffraction, 2 ligands (GEH, MG), 1 pocket (best druggability 0.42). MolNFT v1 #151403 on…
- PDB
- 6HMT
- Type
- protein
- Length
- 241 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; Estrogen receptor
- UniProt
- P31947
- Ligands
- GEH, MG
- Pockets
- 1 · best druggability 0.42
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 | 81% helix, 0% strand | P31947 |
| B | Estrogen receptor | protein | 5 | 0% helix, 0% strand | — |
Ligands and binding sites
- GEH · 2-(4-chloranylphenoxy)-2-methyl-~{N}-(2-sulfanylethyl) propanamide · ligand · chains A, B
- MG · Magnesium ion · metal · 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 | 88 | 0.42 | 0.78 | 15 | GEH |
Interfaces
1 interface between chains.
- A–B · 463 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, phosphorylation).
Compared structures
- 6HMT · Ternary complex of Estrogen Receptor alpha peptide and 14-3-3 sigma C42 mutant bound to… · 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 0.95
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 6HMT · PDBe 6HMT · UniProt P31947
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