Research workbench
Stapled-peptides tailored against initiation of translation
Analyse Stapled-peptides tailored against initiation of translation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZJZ
- Type
- protein
- Length
- 195 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P06730
- Ligands
- ACE, MGT, NH2
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 182 | — | P06730 |
| B | — | protein | 13 | — | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A, B
- MGT · 7N-methyl-8-hydroguanosine-5'-triphosphate · ligand · chains A
- NH2 · Amino group · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5ZJZ · Stapled-peptides tailored against initiation of translation · the same entry in another collection · chain A against A, TM-score 1.00
- P06730 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 4E (P06730) · 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 P06730
- Elsewhere: RCSB PDB 5ZJZ · PDBe 5ZJZ · UniProt P06730
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