Research workbench
Crystal structure of the apo form of E. COLI tryptophanase at 1.9 a resolution
Analyse Crystal structure of the apo form of E. COLI tryptophanase at 1.9 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OQX
- Type
- protein
- Length
- 465 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophanase
- EC
- 4.1.99.1
- UniProt
- P0A853
- Ligands
- MG, CL
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophanase (EC 4.1.99.1) | protein | 465 | 46% helix, 14% strand | P0A853 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 253 | 0.64 | 0.82 | 26 | empty |
| 2 | 366 | 0.58 | 0.75 | 38 | empty |
| 3 | 295 | 0.55 | 0.75 | 35 | empty |
| 4 | 182 | 0.51 | 0.78 | 28 | empty |
Modifications
Observed in the structure: 2 modified (artifact).
Compared structures
- 2OQX · Crystal Structure of the apo form of E. coli tryptophanase at 1.9 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P0A853 · AlphaFold monomer V2.0 prediction for tryptophanase (P0A853) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 P0A853
- Elsewhere: RCSB PDB 2OQX · PDBe 2OQX · UniProt P0A853
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.