MolNFT v1 · #128585 · protein
Structural basis for earp-mediated arginine glycosylation of translation elongation factor ef-P
5NV8: “Structural basis for earp-mediated arginine glycosylation of translation elongation factor ef-P”. X-ray diffraction, 1 ligand (TRH). MolNFT v1 #128585 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5NV8
- Type
- protein
- Length
- 303 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q88LS1
- Ligands
- TRH
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 303 | — | Q88LS1 |
Ligands and binding sites
- TRH · 2'-deoxy-thymidine-beta-L-rhamnose · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NV8 · Structural basis for EarP-mediated arginine glycosylation of translation elongation… · the same entry in another collection · chain A against A, TM-score 1.00
- Q88LS1 · AlphaFold monomer V2.0 prediction for protein-arginine rhamnosyltransferase (Q88LS1) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q88LS1
- Elsewhere: RCSB PDB 5NV8 · PDBe 5NV8 · UniProt Q88LS1
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