MolNFT v1 · #8195 · protein + RNA
Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
1GTR · RNA (74-mer): “Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase”. X-ray diffraction, 1 ligand (ATP), 10 pockets (best druggability 0.77). MolNFT v1 #8195 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1GTR
- Type
- protein + RNA
- Length
- 603 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA (74-mer); Glutaminyl-tRNA synthetase
- EC
- 6.1.1.18
- UniProt
- P00962
- Ligands
- ATP
- Pockets
- 10 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | RNA (74-mer) (EC 6.1.1.18) | rna | 74 | — | — |
| A | Glutaminyl-tRNA synthetase | protein | 529 | 32% 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
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 124 | 0.77 | 0.96 | 27 | empty |
| 2 | 759 | 0.75 | 0.80 | 67 | ATP |
| 3 | 734 | 0.67 | 0.76 | 44 | empty |
| 4 | 126 | 0.64 | 0.87 | 25 | empty |
| 5 | 515 | 0.62 | 0.76 | 31 | empty |
Interfaces
1 interface between chains.
- B–A · 2732 Ų buried · 81 hydrogen bonds · protein-nucleic
Compared structures
- 1GTR · Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase · 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 1GTR · PDBe 1GTR · UniProt P00962
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