MolNFT v1 · #26472 · protein
Crystal structure of tryptophan synthase alpha-subunit from escherichia COLI
1WQ5 · Tryptophan synthase alpha chain: “Crystal structure of tryptophan synthase alpha-subunit from escherichia COLI”. X-ray diffraction, 1 ligand (SO4), 8 pockets (best druggability 0.74). MolNFT v1 #26472 on GenesisL1: 3D structure…
- PDB
- 1WQ5
- Type
- protein
- Length
- 519 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophan synthase alpha chain
- EC
- 4.2.1.20
- UniProt
- P0A877
- Ligands
- SO4
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophan synthase alpha chain (EC 4.2.1.20) | protein | 258 | 50% helix, 15% strand | P0A877 |
| B | Tryptophan synthase alpha chain (EC 4.2.1.20) | protein | 261 | 50% helix, 14% strand | P0A877 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1049 | 0.74 | 0.77 | 62 | GOL |
| 2 | 145 | 0.59 | 0.83 | 27 | SO4, GOL |
| 3 | 144 | 0.55 | 0.81 | 30 | GOL |
| 4 | 132 | 0.42 | 0.75 | 20 | empty |
| 5 | 105 | 0.39 | 0.76 | 25 | GOL |
Interfaces
1 interface between chains.
- A–B · 1930 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1WQ5 · Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
- P0A877 · AlphaFold monomer V2.0 prediction for tryptophan synthase alpha chain (P0A877) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P0A877
- Elsewhere: RCSB PDB 1WQ5 · PDBe 1WQ5 · UniProt P0A877
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