MolNFT v2 · #219249 · protein
TRYPTOPHAN SYNTHASE measured via serial crystallography from a kapton HARE-chip (125 micron)
8RSZ · Tryptophan synthase alpha chain: “TRYPTOPHAN SYNTHASE measured via serial crystallography from a kapton HARE-chip (125 micron)”. X-ray diffraction at 2.2, 2 ligands (CS, CL), 5 pockets (best druggability 0.71). MolNFT v2 #219249 on…
- PDB
- 8RSZ
- Type
- protein
- Length
- 650 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Salmonella enterica subsp. enterica serovar Typhimurium
- Molecule
- Tryptophan synthase alpha chain; Tryptophan synthase beta chain
- EC
- 4.2.1.20
- UniProt
- P00929, P0A2K1
- Ligands
- CS, CL
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · resolution 2.2 · 2 distinct chains · 49% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophan synthase alpha chain (EC 4.2.1.20) | protein | 256 | 52% helix, 14% strand | P00929 |
| E | Tryptophan synthase beta chain (EC 4.2.1.20) | protein | 394 | 47% helix, 22% strand | P0A2K1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 279 | 0.71 | 0.85 | 45 | empty |
| 2 | 353 | 0.66 | 0.80 | 36 | empty |
| 3 | 75 | 0.40 | 0.79 | 15 | empty |
| 4 | 97 | 0.39 | 0.76 | 20 | empty |
| 5 | 51 | 0.32 | 0.78 | 11 | empty |
Interfaces
1 interface between chains.
- A–E · 1351 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (cofactor).
Compared structures
- P00929 · AlphaFold monomer V2.0 prediction for tryptophan synthase alpha chain (P00929) · 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 P00929
- Every structure of UniProt P0A2K1
- Elsewhere: RCSB PDB 8RSZ · PDBe 8RSZ · UniProt P00929 · UniProt P0A2K1
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