MolNFT v1 · #134521 · protein
Structure of the catalytic domain of the class I polyhydroxybutyrate synthase from cupriavidus necator
5T6O · Poly-beta-hydroxybuterate polymerase: “Structure of the catalytic domain of the class I polyhydroxybutyrate synthase from cupriavidus necator”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.61). MolNFT v1 #134521…
- PDB
- 5T6O
- Type
- protein
- Length
- 379 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Poly-beta-hydroxybuterate polymerase
- UniProt
- D3UAK8
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Poly-beta-hydroxybuterate polymerase | protein | 379 | 36% helix, 20% strand | D3UAK8 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains 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 | 135 | 0.61 | 0.85 | 31 | empty |
| 2 | 207 | 0.50 | 0.76 | 35 | empty |
| 3 | 67 | 0.38 | 0.79 | 16 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 D3UAK8
- Elsewhere: RCSB PDB 5T6O · PDBe 5T6O · UniProt D3UAK8
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