Research workbench
Crystal structure of tryptophan synthase beta chain from thermus thermophilus HB8
Analyse Crystal structure of tryptophan synthase beta chain from thermus thermophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X1Q
- Type
- protein
- Length
- 739 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophan synthase beta chain
- EC
- 4.2.1.20
- UniProt
- P16609
- Ligands
- CL
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophan synthase beta chain (EC 4.2.1.20) | protein | 385 | 48% helix, 18% strand | P16609 |
| B | Tryptophan synthase beta chain (EC 4.2.1.20) | protein | 354 | 48% helix, 15% strand | P16609 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1121 | 0.79 | 0.81 | 128 | empty |
| 2 | 51 | 0.68 | 0.97 | 17 | empty |
| 3 | 51 | 0.67 | 0.97 | 18 | empty |
| 4 | 140 | 0.56 | 0.82 | 22 | empty |
| 5 | 218 | 0.52 | 0.76 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 1779 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 modified (engineered).
Compared structures
- 1X1Q · Crystal structure of tryptophan synthase beta chain from Thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00
- P16609 · AlphaFold monomer V2.0 prediction for tryptophan synthase beta chain (P16609) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P16609
- Elsewhere: RCSB PDB 1X1Q · PDBe 1X1Q · UniProt P16609
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