Research workbench
Glutaminyl-tRNA synthetase mutant I129T complexed with glutamine transfer RNA
Analyse Glutaminyl-tRNA synthetase mutant I129T complexed with glutamine transfer RNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QRU
- Type
- protein + RNA
- Length
- 603 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TRNAGLN2; Protein (glutaminyl-tRNA synthetase (E.C.6.1.1.18))
- EC
- 6.1.1.18
- UniProt
- P00962
- Ligands
- ATP
- Pockets
- 9 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | TRNAGLN2 | rna | 74 | — | — |
| A | Protein (glutaminyl-tRNA synthetase (E.C.6.1.1.18)) (EC 6.1.1.18) | protein | 529 | 31% helix, 25% strand | P00962 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1048 | 0.78 | 0.81 | 92 | ATP |
| 2 | 141 | 0.77 | 0.95 | 23 | empty |
| 3 | 123 | 0.67 | 0.90 | 24 | empty |
| 4 | 704 | 0.67 | 0.76 | 43 | empty |
| 5 | 210 | 0.55 | 0.79 | 31 | empty |
Interfaces
1 interface between chains.
- B–A · 2692 Ų buried · 80 hydrogen bonds · protein-nucleic
Compared structures
- 1QRU · Glutaminyl-tRNA synthetase mutant I129T complexed with glutamine transfer RNA · the same entry in another collection · chain B against B, TM-score 1.00
- P00962 · AlphaFold monomer V2.0 prediction for glutamine--tRNA ligase (P00962) · 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 P00962
- Elsewhere: RCSB PDB 1QRU · PDBe 1QRU · UniProt P00962
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