MolNFT v1 · #129464 · protein
Structure of human mitochondrial transcription elongation factor (tefm) C-terminal domain
5OL8 · Transcription elongation factor, mitochondrial: “Structure of human mitochondrial transcription elongation factor (tefm) C-terminal domain”. X-ray diffraction, 11 pockets (best druggability 0.70). MolNFT v1 #129464 on GenesisL1: 3D…
- PDB
- 5OL8
- Type
- protein
- Length
- 820 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription elongation factor, mitochondrial
- UniProt
- Q96QE5
- Pockets
- 11 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transcription elongation factor, mitochondrial | protein | 205 | 42% helix, 20% strand | Q96QE5 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains A, B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 668 | 0.70 | 0.78 | 63 | empty |
| 2 | 159 | 0.56 | 0.81 | 24 | GOL |
| 3 | 156 | 0.56 | 0.81 | 28 | GOL |
| 4 | 134 | 0.56 | 0.82 | 25 | GOL |
| 5 | 194 | 0.53 | 0.78 | 30 | GOL |
Interfaces
3 interfaces between chains.
- A–B · 1150 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 1138 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 557 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5OL8 · Structure of human mitochondrial transcription elongation factor (TEFM) C-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 0.98
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 5OL8 · PDBe 5OL8 · UniProt Q96QE5
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