MolNFT v1 · #100766 · protein
Crystal structure of 14-3-3ZETA in complex with a peptide derived from exos
4N7G · 14-3-3 protein ZETA/DELTA: “Crystal structure of 14-3-3ZETA in complex with a peptide derived from exos”. X-ray diffraction. MolNFT v1 #100766 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4N7G
- Type
- protein
- Length
- 240 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein ZETA/DELTA; Exoenzyme S
- UniProt
- P63104, Q93SQ3
Structure
x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein ZETA/DELTA | protein | 229 | 81% helix, 0% strand | P63104 |
| B | Exoenzyme S | protein | 11 | 45% helix, 0% strand | Q93SQ3 |
Ligands and binding sites
- P6G · Hexaethylene glycol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 714 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4N7G · Crystal structure of 14-3-3zeta in complex with a peptide derived from ExoS · 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 0.98
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 P63104
- Every structure of UniProt Q93SQ3
- Elsewhere: RCSB PDB 4N7G · PDBe 4N7G · UniProt P63104 · UniProt Q93SQ3
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