MolNFT v2 · #138604 · protein
Crystal Structure of L-Threonine Aldolase from Pseudomonas putida
5VYE: “Crystal Structure of L-Threonine Aldolase from Pseudomonas putida”. X-ray diffraction at 2.275, 1 ligand (PLR). MolNFT v2 #138604 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5VYE
- Type
- protein
- Length
- 1,371 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.275
- Source
- Pseudomonas putida
- UniProt
- A0A166JNM8
- Ligands
- PLR
Structure
x-ray diffraction · resolution 2.275 · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 343 | — | A0A166JNM8 |
| B | — | protein | 344 | — | A0A166JNM8 |
| C, D | — | protein | 342 | — | A0A166JNM8 |
Ligands and binding sites
- PLR · (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate · ligand · 4 copies · chains A, B, C, D
- GOL · Glycerol · additive · 4 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5VYE · Crystal structure of L-threonine aldolase from pseudomonas putida · the same entry in another collection · 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 A0A166JNM8
- Elsewhere: RCSB PDB 5VYE · PDBe 5VYE · UniProt A0A166JNM8
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