MolNFT v1 · #126260 · protein
F420-dependent glucose-6-phosphate dehydrogenase from rhodococcus jostii RHA1
5LXE · F420-dependent glucose-6-phosphate dehydrogenase 1: “F420-dependent glucose-6-phosphate dehydrogenase from rhodococcus jostii RHA1”. X-ray diffraction, 1 ligand (SO4), 5 pockets (best druggability 0.72). MolNFT v1 #126260 on…
- PDB
- 5LXE
- Type
- protein
- Length
- 628 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F420-dependent glucose-6-phosphate dehydrogenase 1
- EC
- 1.1.98.2
- UniProt
- Q0RVH7
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F420-dependent glucose-6-phosphate dehydrogenase 1 (EC 1.1.98.2) | protein | 324 | 46% helix, 17% strand | Q0RVH7 |
| B | F420-dependent glucose-6-phosphate dehydrogenase 1 (EC 1.1.98.2) | protein | 304 | 46% helix, 17% strand | Q0RVH7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.72 | 0.97 | 20 | empty |
| 2 | 674 | 0.69 | 0.77 | 59 | empty |
| 3 | 394 | 0.61 | 0.77 | 41 | GOL |
| 4 | 352 | 0.57 | 0.76 | 34 | empty |
| 5 | 75 | 0.30 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2041 Ų buried · 35 hydrogen bonds · protein-protein
Compared structures
- 5LXE · F420-dependent glucose-6-phosphate dehydrogenase from Rhodococcus jostii RHA1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q0RVH7 · AlphaFold monomer V2.0 prediction for F420-dependent glucose-6-phosphate dehydrogenase 1… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q0RVH7
- Elsewhere: RCSB PDB 5LXE · PDBe 5LXE · UniProt Q0RVH7
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