Research workbench
Crystal structure of human MTERF1 bound to the termination sequence
Analyse Crystal structure of human MTERF1 bound to the termination sequence in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MVA
- Type
- protein + DNA
- Length
- 368 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription termination factor, mitochondrial…
- UniProt
- Q99551
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| O | Transcription termination factor, mitochondrial | protein | 324 | 73% helix, 0% strand | Q99551 |
| D | 5'-D(*AP*TP*TP*AP*CP*CP*GP*GP*GP*CP*TP*CP*TP*GP*CP*CP*AP*TP *CP*TP*TP*A)-3') | dna | 22 | — | — |
| E | 5'-D(*TP*AP*AP*GP*AP*TP*GP*GP*CP*AP*GP*AP*GP*CP*CP*CP*GP*GP *TP*AP*AP*T)-3') | dna | 22 | — | — |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 776 | 0.78 | 0.82 | 60 | empty |
| 2 | 187 | 0.56 | 0.80 | 21 | empty |
| 3 | 65 | 0.25 | 0.71 | 12 | empty |
Interfaces
3 interfaces between chains.
- O–E · 1412 Ų buried · 33 hydrogen bonds · protein-nucleic
- O–D · 955 Ų buried · 21 hydrogen bonds · protein-nucleic
- D–E · 939 Ų buried · 94 hydrogen bonds · nucleic-nucleic
Compared structures
- 3MVA · Crystal structure of human MTERF1 bound to the termination sequence · the same entry in another collection · chain O against O, TM-score 1.00
- Q99551 · AlphaFold monomer V2.0 prediction for transcription termination factor 1, mitochondrial… · a predicted model of the same protein · chain O against A, TM-score 1.00
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 Q99551
- Elsewhere: RCSB PDB 3MVA · PDBe 3MVA · UniProt Q99551
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