MolNFT v1 · #106850 · protein
Crystal structure of a deletion mutant of a tyrosyl-T/RNA synthetase complexed with tyrosine
4TS1 · Tyrosyl-tRNA synthetase: “Crystal structure of a deletion mutant of a tyrosyl-T/RNA synthetase complexed with tyrosine”. X-ray diffraction, 1 ligand (TYR), 2 pockets (best druggability 0.69). MolNFT v1 #106850 on GenesisL1: 3D…
- PDB
- 4TS1
- Type
- protein
- Length
- 628 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosyl-tRNA synthetase
- EC
- 6.1.1.1
- UniProt
- P00952
- Ligands
- TYR
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosyl-tRNA synthetase (EC 6.1.1.1) | protein | 317 | 52% helix, 12% strand | P00952 |
| B | Tyrosyl-tRNA synthetase (EC 6.1.1.1) | protein | 311 | 52% helix, 12% strand | P00952 |
Ligands and binding sites
- TYR · Tyrosine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 397 | 0.69 | 0.81 | 47 | TYR |
| 2 | 339 | 0.65 | 0.80 | 34 | TYR |
Interfaces
1 interface between chains.
- A–B · 1552 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 4TS1 · Crystal structure of a deletion mutant of a tyrosyl-T/RNA synthetase complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P00952 · AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (P00952) · 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 P00952
- Elsewhere: RCSB PDB 4TS1 · PDBe 4TS1 · UniProt P00952
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