Research workbench
Sulfolobus solfataricus tryptophan synthase B2O
Analyse Sulfolobus solfataricus tryptophan synthase B2O in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EQN
- Type
- protein
- Length
- 823 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophan synthase beta chain 2
- EC
- 4.2.1.20
- UniProt
- Q97TX6
- Ligands
- PLP
- Pockets
- 8 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Tryptophan synthase beta chain 2 (EC 4.2.1.20) | protein | 407 | 43% helix, 19% strand | Q97TX6 |
| D | Tryptophan synthase beta chain 2 (EC 4.2.1.20) | protein | 416 | 44% helix, 18% strand | Q97TX6 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 594 | 0.80 | 0.86 | 70 | PLP |
| 2 | 647 | 0.80 | 0.85 | 66 | PLP |
| 3 | 113 | 0.78 | 0.97 | 25 | empty |
| 4 | 225 | 0.60 | 0.80 | 35 | empty |
| 5 | 75 | 0.50 | 0.83 | 19 | empty |
Interfaces
1 interface between chains.
- B–D · 2339 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- Q97TX6 · AlphaFold monomer V2.0 prediction for tryptophan synthase beta chain 2 (Q97TX6) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q97TX6
- Elsewhere: RCSB PDB 6EQN · PDBe 6EQN · UniProt Q97TX6
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