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Structure of E. cuniculi MTQ2-TRM112 complex responible for the methylation of ERF1 translation termination factor
Analyse Structure of E. cuniculi MTQ2-TRM112 complex responible for the methylation of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q87
- Type
- protein
- Length
- 286 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein ECU08_1170; N6 adenine specific DNA methylase
- UniProt
- Q8SUP0, Q8SRR4
- Ligands
- SAM, ZN
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative uncharacterized protein ECU08_1170 | protein | 122 | 33% helix, 25% strand | Q8SUP0 |
| B | N6 adenine specific DNA methylase | protein | 164 | 32% helix, 27% strand | Q8SRR4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.72 | 0.88 | 43 | SAM |
| 2 | 113 | 0.46 | 0.79 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1023 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 3Q87 · Structure of E. cuniculi Mtq2-Trm112 complex responible for the methylation of eRF1… · the same entry in another collection · chain B against B, 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 Q8SUP0
- Every structure of UniProt Q8SRR4
- Elsewhere: RCSB PDB 3Q87 · PDBe 3Q87 · UniProt Q8SUP0 · UniProt Q8SRR4
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