Research workbench
Crystal structure of 14-3-3ZETA in complex with a macrocyclic 8-mer peptide derived from exos
Analyse Crystal structure of 14-3-3ZETA in complex with a macrocyclic 8-mer peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RLZ
- Type
- protein
- Length
- 469 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein ZETA/DELTA; Etme
- UniProt
- P63104
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 3 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein ZETA/DELTA | protein | 227 | 81% helix, 0% strand | P63104 |
| B | 14-3-3 protein ZETA/DELTA | protein | 226 | 73% helix, 0% strand | P63104 |
| C, D | Etme | protein | 8 | 0% helix, 0% strand | — |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 260 | 0.51 | 0.75 | 25 | empty |
| 2 | 97 | 0.36 | 0.74 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 951 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 564 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 513 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (nonstandard).
Compared structures
- 6RLZ · Crystal Structure of 14-3-3zeta in complex with a macrocyclic 8-mer peptide derived from… · the same entry in another collection · chain A against A, 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 A against A, TM-score 0.97
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 6RLZ · PDBe 6RLZ · UniProt P63104
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