Research workbench
Fitting of ef-tu and tRNA in the low resolution cryo-EM MAP of an ef- tu ternary complex (GDP and kirromycin) bound to E. COLI 70S ribosome
Analyse Fitting of ef-tu and tRNA in the low resolution cryo-EM MAP of an ef- tu… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LS2
- Type
- protein
- Length
- 386 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor tu
- UniProt
- P0A6N1
- Pockets
- 3 · best druggability 0.37
Structure
electron microscopy · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor tu | protein | 386 | 0% helix, 0% strand | P0A6N1 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.37 | 0.73 | 32 | empty |
| 2 | 67 | 0.29 | 0.71 | 19 | empty |
| 3 | 53 | 0.28 | 0.73 | 17 | empty |
Compared structures
- 1LS2 · Fitting of EF-Tu and tRNA in the Low Resolution Cryo-EM Map of an EF-Tu Ternary Complex… · the same entry in another collection · chain A against A, TM-score 1.00
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 P0A6N1
- Elsewhere: RCSB PDB 1LS2 · PDBe 1LS2 · UniProt P0A6N1
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