Research workbench
Crystal structure of apo-wildtype glycyl-tRNA synthetase
Analyse Crystal structure of apo-wildtype glycyl-tRNA synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q5H
- Type
- protein
- Length
- 528 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycyl-tRNA synthetase
- EC
- 6.1.1.14
- UniProt
- P41250
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycyl-tRNA synthetase (EC 6.1.1.14) | protein | 528 | 37% helix, 25% strand | P41250 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1151 | 0.74 | 0.77 | 86 | empty |
| 2 | 56 | 0.42 | 0.82 | 17 | empty |
| 3 | 75 | 0.38 | 0.78 | 17 | empty |
| 4 | 55 | 0.31 | 0.76 | 11 | empty |
| 5 | 59 | 0.29 | 0.74 | 15 | empty |
Compared structures
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 P41250
- Elsewhere: RCSB PDB 2Q5H · PDBe 2Q5H · UniProt P41250
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