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Crystal structure of a C-terminal fragment of moorella thermoacetica elongation factor selb
Analyse Crystal structure of a C-terminal fragment of moorella thermoacetica elongation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LVA
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Selenocysteine-specific elongation factor
- UniProt
- Q46455
- Ligands
- Y1, SO4
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Selenocysteine-specific elongation factor | protein | 258 | 57% helix, 16% strand | Q46455 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (engineered).
Compared structures
- 1LVA · Crystal structure of a C-terminal fragment of Moorella thermoacetica elongation factor… · the same entry in another collection · chain A against A, TM-score 1.00
- Q46455 · AlphaFold monomer V2.0 prediction for selenocysteine-specific elongation factor (Q46455) · a predicted model of the same protein · chain A against A, TM-score 0.76
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 Q46455
- Elsewhere: RCSB PDB 1LVA · PDBe 1LVA · UniProt Q46455
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