Research workbench
Structure of 14-3-3 gamma in complex with NEDD4-2 14-3-3 binding motif SER342
Analyse Structure of 14-3-3 gamma in complex with NEDD4-2 14-3-3 binding motif SER342 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZBT
- Type
- protein
- Length
- 941 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein gamma; E3 ubiquitin-protein ligase NEDD4-like
- EC
- 2.3.2.26
- UniProt
- P61981, Q96PU5
- Ligands
- CFH
- Pockets
- 14 · best druggability 0.68
Structure
x-ray diffraction · 6 distinct chains · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein gamma | protein | 232 | 83% helix, 0% strand | P61981 |
| B | 14-3-3 protein gamma | protein | 227 | 82% helix, 0% strand | P61981 |
| C | 14-3-3 protein gamma | protein | 227 | 82% helix, 0% strand | P61981 |
| D | 14-3-3 protein gamma | protein | 229 | 84% helix, 0% strand | P61981 |
| E, F | E3 ubiquitin-protein ligase NEDD4-like (EC 2.3.2.26) | protein | 7 | 0% helix, 0% strand | Q96PU5 |
| G, H | E3 ubiquitin-protein ligase NEDD4-like (EC 2.3.2.26) | protein | 6 | 0% helix, 0% strand | Q96PU5 |
Ligands and binding sites
- CFH · 1,1,1,3,3,3-hexafluoropropan-2-ol · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 558 | 0.68 | 0.78 | 42 | empty |
| 2 | 543 | 0.68 | 0.78 | 54 | empty |
| 3 | 77 | 0.68 | 0.93 | 17 | CFH |
| 4 | 556 | 0.67 | 0.78 | 45 | empty |
| 5 | 80 | 0.67 | 0.92 | 15 | CFH |
Interfaces
11 interfaces between chains.
- A–B · 1000 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 983 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 949 Ų buried · 12 hydrogen bonds · protein-protein
- C–F · 513 Ų buried · 11 hydrogen bonds · protein-protein
- A–E · 449 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 6ZBT · Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser342 · the same entry in another collection · chain H against H, TM-score 1.00
- P61981 · AlphaFold monomer V2.0 prediction for 14-3-3 protein gamma (P61981) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P61981
- Every structure of UniProt Q96PU5
- Elsewhere: RCSB PDB 6ZBT · PDBe 6ZBT · UniProt P61981 · UniProt Q96PU5
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