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Crystal structure of human mitochondrial transcription termination factor 3
Analyse Crystal structure of human mitochondrial transcription termination factor 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M66
- Type
- protein
- Length
- 270 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mterf domain-containing protein 1, mitochondrial
- UniProt
- Q96E29
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mterf domain-containing protein 1, mitochondrial | protein | 270 | 73% helix, 0% strand | Q96E29 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.34 | 0.76 | 18 | empty |
| 2 | 50 | 0.32 | 0.77 | 12 | empty |
Compared structures
- 3M66 · Crystal structure of human Mitochondrial Transcription Termination Factor 3 · the same entry in another collection · chain A against A, TM-score 1.00
- Q96E29 · AlphaFold monomer V2.0 prediction for transcription termination factor 3, mitochondrial… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q96E29
- Elsewhere: RCSB PDB 3M66 · PDBe 3M66 · UniProt Q96E29
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