Research workbench
Structure of a translation elongation factor P (efp) from coxiella burnetii
Analyse Structure of a translation elongation factor P (efp) from coxiella burnetii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TRE
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor P
- UniProt
- Q83AR4
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor P | protein | 129 | 10% helix, 53% strand | Q83AR4 |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 3TRE · Structure of a translation elongation factor P (efp) from Coxiella burnetii · the same entry in another collection · chain A against A, TM-score 1.00
- Q83AR4 · AlphaFold monomer V2.0 prediction for elongation factor P (Q83AR4) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q83AR4
- Elsewhere: RCSB PDB 3TRE · PDBe 3TRE · UniProt Q83AR4
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