Research workbench
Transition-state model conformation of the switch I region fitted into the cryo-EM MAP of the EEF2.80S.ALF4.GDP complex
Analyse Transition-state model conformation of the switch I region fitted into the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DWU
- Type
- protein
- Length
- 46 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor tu-B
- UniProt
- P60339
Structure
electron microscopy · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor tu-B | protein | 46 | 0% helix, 0% strand | P60339 |
Compared structures
- 3DWU · Transition-state model conformation of the switch I region fitted into the cryo-EM map of… · the same entry in another collection · chain A against A, TM-score 1.00
- P60339 · AlphaFold monomer V2.0 prediction for elongation factor tu-B (P60339) · a predicted model of the same protein · chain A against A, TM-score 0.64
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 P60339
- Elsewhere: RCSB PDB 3DWU · PDBe 3DWU · UniProt P60339
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