Research workbench
Structure of human mitochondrial transcription elongation factor (tefm) N-terminal domain
Analyse Structure of human mitochondrial transcription elongation factor (tefm)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OL9
- Type
- protein
- Length
- 81 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription elongation factor, mitochondrial
- UniProt
- Q96QE5
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription elongation factor, mitochondrial | protein | 81 | 69% helix, 0% strand | Q96QE5 |
Ligands and binding sites
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OL9 · Structure of human mitochondrial transcription elongation factor (TEFM) N-terminal domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q96QE5 · AlphaFold monomer V2.0 prediction for transcription elongation factor, mitochondrial… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q96QE5
- Elsewhere: RCSB PDB 5OL9 · PDBe 5OL9 · UniProt Q96QE5
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