Research workbench
Crystal structure of archaeoglobus fulgidus alanyl-tRNA synthetase lacking the C-terminal dimerization domain in complex with ala-sa
Analyse Crystal structure of archaeoglobus fulgidus alanyl-tRNA synthetase lacking the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZTG
- Type
- protein
- Length
- 739 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alanyl-tRNA synthetase
- EC
- 6.1.1.7
- UniProt
- O28029
- Ligands
- A5A, ZN
- Pockets
- 10 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alanyl-tRNA synthetase (EC 6.1.1.7) | protein | 739 | 38% helix, 24% strand | O28029 |
Ligands and binding sites
- A5A · 5'-O-(N-(L-alanyl)-sulfamoyl)adenosine · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains 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, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1070 | 0.79 | 0.80 | 84 | empty |
| 2 | 678 | 0.72 | 0.79 | 65 | A5A |
| 3 | 57 | 0.70 | 0.97 | 16 | empty |
| 4 | 303 | 0.60 | 0.78 | 41 | empty |
| 5 | 249 | 0.57 | 0.78 | 25 | empty |
Modifications
Observed in the structure: 15 modified (engineered).
Compared structures
- 2ZTG · Crystal structure of Archaeoglobus fulgidus alanyl-tRNA synthetase lacking the C-terminal… · the same entry in another collection · chain A against A, TM-score 1.00
- O28029 · AlphaFold monomer V2.0 prediction for alanine--tRNA ligase (O28029) · 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 O28029
- Elsewhere: RCSB PDB 2ZTG · PDBe 2ZTG · UniProt O28029
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