Research workbench
Structure of mutant tryptophan synthase alpha-subunit (E74A) from a hyperthermophile, pyrococcus furiosus
Analyse Structure of mutant tryptophan synthase alpha-subunit (E74A) from a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E09
- Type
- protein
- Length
- 489 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
- Q8U094
- Pockets
- 6 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophan synthase alpha chain (EC 4.2.1.20) | protein | 244 | 50% helix, 16% strand | Q8U094 |
| B | Tryptophan synthase alpha chain (EC 4.2.1.20) | protein | 245 | 50% helix, 16% strand | Q8U094 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 578 | 0.67 | 0.77 | 47 | empty |
| 2 | 205 | 0.61 | 0.82 | 36 | empty |
| 3 | 206 | 0.61 | 0.82 | 32 | empty |
| 4 | 186 | 0.42 | 0.73 | 27 | empty |
| 5 | 111 | 0.41 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 582 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2E09 · Structure of mutant tryptophan synthase alpha-subunit (E74A) from a hyperthermophile… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8U094 · AlphaFold monomer V2.0 prediction for tryptophan synthase alpha chain (Q8U094) · a predicted model of the same protein · chain A 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 Q8U094
- Elsewhere: RCSB PDB 2E09 · PDBe 2E09 · UniProt Q8U094
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