Research workbench
Structure of 14-3-3 zeta in complex with CAMKK2 14-3-3 binding motif
Analyse Structure of 14-3-3 zeta in complex with CAMKK2 14-3-3 binding motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EWW
- Type
- protein
- Length
- 910 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein ZETA/DELTA; Arg-lys-leu-sep-leu-gln-glu-arg
- UniProt
- P63104
- Pockets
- 12 · best druggability 0.80
Structure
x-ray diffraction · 6 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein ZETA/DELTA | protein | 217 | 83% helix, 0% strand | P63104 |
| C | 14-3-3 protein ZETA/DELTA | protein | 221 | 81% helix, 0% strand | P63104 |
| B | 14-3-3 protein ZETA/DELTA | protein | 222 | 84% helix, 0% strand | P63104 |
| D | 14-3-3 protein ZETA/DELTA | protein | 219 | 82% helix, 0% strand | P63104 |
| E, F, G | Arg-lys-leu-sep-leu-gln-glu-arg | protein | 8 | 0% helix, 0% strand | — |
| H | Arg-lys-leu-sep-leu-gln-glu-arg | protein | 7 | 0% helix, 0% strand | — |
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 533 | 0.80 | 0.87 | 48 | empty |
| 2 | 113 | 0.60 | 0.87 | 30 | empty |
| 3 | 94 | 0.59 | 0.87 | 20 | empty |
| 4 | 203 | 0.59 | 0.81 | 32 | empty |
| 5 | 222 | 0.58 | 0.80 | 24 | empty |
Interfaces
14 interfaces between chains.
- A–B · 1067 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 1038 Ų buried · 11 hydrogen bonds · protein-protein
- A–E · 650 Ų buried · 15 hydrogen bonds · protein-protein
- B–F · 565 Ų buried · 15 hydrogen bonds · protein-protein
- C–G · 504 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 6EWW · Structure of 14-3-3 zeta in complex with CaMKK2 14-3-3 binding motif · the same entry in another collection · chain H against H, TM-score 1.00
- P63104 · AlphaFold monomer V2.0 prediction for 14-3-3 protein ZETA/DELTA (P63104) · a predicted model of the same protein · chain B 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 P63104
- Elsewhere: RCSB PDB 6EWW · PDBe 6EWW · UniProt P63104
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