MolNFT v1 · #143892 · protein
Complex of 14-3-3 theta with an IRSP53 peptide phosphorylated at S366
6BD1 · 14-3-3 protein theta: “Complex of 14-3-3 theta with an IRSP53 peptide phosphorylated at S366”. X-ray diffraction, 1 ligand (MG), 10 pockets (best druggability 0.75). MolNFT v1 #143892 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6BD1
- Type
- protein
- Length
- 946 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein theta; Insulin receptor substrate protein of 53 kda, peptide (IRSP53)
- UniProt
- Q3SZI4
- Ligands
- MG
- Pockets
- 10 · best druggability 0.75
Structure
x-ray diffraction · 4 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein theta | protein | 229 | 84% helix, 0% strand | Q3SZI4 |
| B, E, F | 14-3-3 protein theta | protein | 230 | 82% helix, 0% strand | Q3SZI4 |
| C, G, H | Insulin receptor substrate protein of 53 kda, peptide (IRSP53) | protein | 7 | 0% helix, 0% strand | — |
| D | Insulin receptor substrate protein of 53 kda, peptide (IRSP53) | protein | 6 | 0% helix, 0% strand | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A, E, B, F
- PEG · Di(hydroxyethyl)ether · additive · 5 copies · chains B, E, F
- 1PE · Pentaethylene glycol · additive · 2 copies · chains A, B, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 719 | 0.75 | 0.80 | 62 | PEG |
| 2 | 505 | 0.66 | 0.78 | 52 | MG |
| 3 | 109 | 0.56 | 0.84 | 23 | empty |
| 4 | 171 | 0.56 | 0.80 | 25 | empty |
| 5 | 181 | 0.55 | 0.79 | 25 | empty |
Interfaces
9 interfaces between chains.
- A–B · 1045 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 1020 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 621 Ų buried · 16 hydrogen bonds · protein-protein
- E–G · 607 Ų buried · 16 hydrogen bonds · protein-protein
- F–H · 583 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 6BD1 · Complex of 14-3-3 theta with an IRSp53 peptide phosphorylated at S366 · the same entry in another collection · chain H against H, TM-score 1.00
- Q3SZI4 · AlphaFold monomer V2.0 prediction for 14-3-3 protein theta (Q3SZI4) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q3SZI4
- Elsewhere: RCSB PDB 6BD1 · PDBe 6BD1 · UniProt Q3SZI4
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