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Crystal structure of the archaeal tRNA M2G/M22G10 methyltransferase (ATRM11) from thermococcus kodakarensis
Analyse Crystal structure of the archaeal tRNA M2G/M22G10 methyltransferase (ATRM11)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5E71
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N2, N2-dimethylguanosine tRNA methyltransferase
- UniProt
- Q5JID5
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N2, N2-dimethylguanosine tRNA methyltransferase | protein | 323 | 34% helix, 32% strand | Q5JID5 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 154 | 0.57 | 0.82 | 33 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5E71 · Crystal structure of the archaeal tRNA m2G/m22G10 methyltransferase (aTrm11) from… · the same entry in another collection · chain A 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 Q5JID5
- Elsewhere: RCSB PDB 5E71 · PDBe 5E71 · UniProt Q5JID5
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