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Crystal structure of L-threonine-O-3-phosphate decarboxylase from S. enterica complexed with its reaction intermediate
Analyse Crystal structure of L-threonine-O-3-phosphate decarboxylase from S. enterica… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LC8
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-threonine-O-3-phosphate decarboxylase
- UniProt
- P97084
- Ligands
- 33P
- Pockets
- 6 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-threonine-O-3-phosphate decarboxylase | protein | 356 | 42% helix, 16% strand | P97084 |
Ligands and binding sites
- 33P · {3-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-2-methyl-propyl}-phosphonic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.63 | 0.83 | 26 | 33P |
| 2 | 111 | 0.45 | 0.79 | 24 | empty |
| 3 | 65 | 0.38 | 0.79 | 22 | empty |
| 4 | 61 | 0.36 | 0.78 | 19 | empty |
| 5 | 60 | 0.33 | 0.77 | 14 | empty |
Compared structures
- 1LC8 · Crystal Structure of L-Threonine-O-3-phosphate Decarboxylase from S. enterica complexed… · the same entry in another collection · chain A against A, TM-score 1.00
- P97084 · AlphaFold monomer V2.0 prediction for threonine-phosphate decarboxylase (P97084) · a predicted model of the same protein · chain A 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 P97084
- Elsewhere: RCSB PDB 1LC8 · PDBe 1LC8 · UniProt P97084
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