Research workbench
Crystal structure of low-specificity L-threonine aldolase from escherichia COLI
Analyse Crystal structure of low-specificity L-threonine aldolase from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WLX
- Type
- protein
- Length
- 663 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Low specificity L-threonine aldolase
- EC
- 4.1.2.48
- UniProt
- P75823
- Ligands
- PLG
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Low specificity L-threonine aldolase (EC 4.1.2.48) | protein | 332 | 44% helix, 18% strand | P75823 |
| A | Low specificity L-threonine aldolase (EC 4.1.2.48) | protein | 331 | 44% helix, 18% strand | P75823 |
Ligands and binding sites
- PLG · N-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane] · ligand · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 225 | 0.63 | 0.83 | 36 | PLG |
| 2 | 204 | 0.61 | 0.83 | 36 | PLG |
| 3 | 59 | 0.29 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- B–A · 1843 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 3WLX · Crystal structure of low-specificity L-threonine aldolase from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
- P75823 · AlphaFold monomer V2.0 prediction for low specificity L-threonine aldolase (P75823) · a predicted model of the same protein · chain B against A, TM-score 1.00
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 P75823
- Elsewhere: RCSB PDB 3WLX · PDBe 3WLX · UniProt P75823
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