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Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif SER164
Analyse Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif SER164 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GKG
- Type
- protein
- Length
- 1,839 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein gamma; Caspase-2
- EC
- 3.4.22.55
- UniProt
- P61981
- Pockets
- 20 · best druggability 0.72
Structure
x-ray diffraction · 9 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E | 14-3-3 protein gamma | protein | 233 | 81% helix, 0% strand | P61981 |
| C | 14-3-3 protein gamma | protein | 231 | 81% helix, 0% strand | P61981 |
| D, G | 14-3-3 protein gamma | protein | 220 | 80% helix, 0% strand | P61981 |
| F | 14-3-3 protein gamma | protein | 226 | 82% helix, 0% strand | P61981 |
| H | 14-3-3 protein gamma | protein | 216 | 80% helix, 0% strand | P61981 |
| I | Caspase-2 (EC 3.4.22.55) | protein | 6 | 0% helix, 0% strand | — |
| J, K, L | Caspase-2 (EC 3.4.22.55) | protein | 3 | 0% helix, 0% strand | — |
| M | Caspase-2 (EC 3.4.22.55) | protein | 7 | 0% helix, 0% strand | — |
| N | Caspase-2 (EC 3.4.22.55) | protein | 5 | 0% helix, 0% strand | — |
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 318 | 0.72 | 0.85 | 49 | empty |
| 2 | 629 | 0.70 | 0.78 | 65 | empty |
| 3 | 675 | 0.69 | 0.77 | 66 | empty |
| 4 | 452 | 0.67 | 0.79 | 54 | empty |
| 5 | 801 | 0.65 | 0.73 | 62 | empty |
Interfaces
17 interfaces between chains.
- A–E · 1096 Ų buried · 15 hydrogen bonds · protein-protein
- B–F · 1076 Ų buried · 14 hydrogen bonds · protein-protein
- D–H · 961 Ų buried · 11 hydrogen bonds · protein-protein
- C–G · 929 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 787 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (phosphorylation).
Compared structures
- 6GKG · Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif Ser164 · the same entry in another collection · chain L against L, TM-score 1.00
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
- Elsewhere: RCSB PDB 6GKG · PDBe 6GKG · UniProt P61981
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