Research workbench
Biphenylalanine modified threonyl-tRNA synthetase from pyrococcus abyssi: I11BIF, F42W, Y79A, and F123Y mutant
Analyse Biphenylalanine modified threonyl-tRNA synthetase from pyrococcus abyssi… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4S02
- Type
- protein
- Length
- 138 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Threonine--tRNA ligase
- EC
- 6.1.1.3
- UniProt
- Q9UZ14
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Threonine--tRNA ligase (EC 6.1.1.3) | protein | 138 | 33% helix, 41% strand | Q9UZ14 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.51 | 0.78 | 23 | empty |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 4S02 · Biphenylalanine modified threonyl-tRNA synthetase from Pyrococcus abyssi: I11BIF, F42W… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UZ14 · AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (Q9UZ14) · 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 Q9UZ14
- Elsewhere: RCSB PDB 4S02 · PDBe 4S02 · UniProt Q9UZ14
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