Research workbench
Ef-tu ef-ts complex from thermus thermophilus
Analyse Ef-tu ef-ts complex from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AIP
- Type
- protein
- Length
- 2,269 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P60338, P43895
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 373 | — | P60338 |
| C, D, G | — | protein | 195 | — | P43895 |
| E, F | — | protein | 372 | — | P60338 |
| H | — | protein | 194 | — | P43895 |
Compared structures
- 1AIP · Ef-tu ef-ts complex from thermus thermophilus · the same entry in another collection · chain D against D, TM-score 1.00
- P43895 · AlphaFold monomer V2.0 prediction for elongation factor ts (P43895) · a predicted model of the same protein · chain H against A, TM-score 0.95
- P60338 · AlphaFold monomer V2.0 prediction for elongation factor tu-a (P60338) · a predicted model of the same protein · chain E against A, TM-score 0.56
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 P60338
- Every structure of UniProt P43895
- Elsewhere: RCSB PDB 1AIP · PDBe 1AIP · UniProt P60338 · UniProt P43895
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