Research workbench
Structure of a udp-glucose dehydrogenase from the hyperthermophilic archaeon pyrobaculum islandicum
Analyse Structure of a udp-glucose dehydrogenase from the hyperthermophilic archaeon… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VTF
- Type
- protein
- Length
- 432 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-glucose 6-dehydrogenase
- EC
- 1.1.1.22
- UniProt
- A1RUM9
- Ligands
- UPG
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-glucose 6-dehydrogenase (EC 1.1.1.22) | protein | 432 | 46% helix, 14% strand | A1RUM9 |
Ligands and binding sites
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 | 536 | 0.73 | 0.81 | 57 | UPG |
| 2 | 339 | 0.63 | 0.79 | 42 | empty |
| 3 | 61 | 0.29 | 0.74 | 16 | empty |
Compared structures
- 3VTF · Structure of a UDP-glucose dehydrogenase from the hyperthermophilic archaeon Pyrobaculum… · 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 A1RUM9
- Elsewhere: RCSB PDB 3VTF · PDBe 3VTF · UniProt A1RUM9
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