Research workbench
Crystal structure of bacterial glycyl tRNA synthetase in complex with glycine
Analyse Crystal structure of bacterial glycyl tRNA synthetase in complex with glycine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LU4
- Type
- protein
- Length
- 1,955 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multifunctional fusion protein
- EC
- 6.1.1.14
- UniProt
- A0A0P6Y0P9
- Ligands
- GLY
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multifunctional fusion protein (EC 6.1.1.14) | protein | 978 | 51% helix, 18% strand | A0A0P6Y0P9 |
| B | Multifunctional fusion protein (EC 6.1.1.14) | protein | 977 | 50% helix, 17% strand | A0A0P6Y0P9 |
Ligands and binding sites
- GLY · Glycine · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.79 | 0.98 | 33 | empty |
| 2 | 116 | 0.78 | 0.97 | 30 | empty |
| 3 | 1152 | 0.76 | 0.79 | 94 | empty |
| 4 | 848 | 0.76 | 0.80 | 78 | GLY |
| 5 | 133 | 0.76 | 0.94 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 2879 Ų buried · 39 hydrogen bonds · protein-protein
Compared structures
- 7LU4 · Crystal structure of bacterial glycyl tRNA synthetase in complex with glycine · 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 A0A0P6Y0P9
- Elsewhere: RCSB PDB 7LU4 · PDBe 7LU4 · UniProt A0A0P6Y0P9
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