MolNFT v1 · #35719 · protein
Complex structure of TRM1 from pyrococcus horikoshii with S-adenosyl- L-homocystein
2EJU · N(2),N(2)-dimethylguanosine tRNA methyltransferase: “Complex structure of TRM1 from pyrococcus horikoshii with S-adenosyl- L-homocystein”. X-ray diffraction, 1 ligand (SAH), 2 pockets (best druggability 0.59). MolNFT v1 #35719 on…
- PDB
- 2EJU
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N(2),N(2)-dimethylguanosine tRNA methyltransferase
- EC
- 2.1.1.32
- UniProt
- O59493
- Ligands
- SAH
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N(2),N(2)-dimethylguanosine tRNA methyltransferase (EC 2.1.1.32) | protein | 371 | 39% helix, 28% strand | O59493 |
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 | 161 | 0.59 | 0.83 | 29 | SAH |
| 2 | 52 | 0.26 | 0.73 | 15 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2EJU · Complex structure of Trm1 from Pyrococcus horikoshii with S-adenosyl-L-Homocystein · the same entry in another collection · chain A against A, TM-score 1.00
- O59493 · AlphaFold monomer V2.0 prediction for tRNA (GUANINE(26)-N(2))-dimethyltransferase (O59493) · 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 O59493
- Elsewhere: RCSB PDB 2EJU · PDBe 2EJU · UniProt O59493
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