Research workbench
Structure of the D10N mutant of beta-phosphoglucomutase from lactococcus lactis inhibited with glucose 6-phosphate and tetrafluoroaluminate to 1.1A resolution.
Analyse Structure of the D10N mutant of beta-phosphoglucomutase from lactococcus lactis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OK2
- Type
- protein
- Length
- 218 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-phosphoglucomutase
- EC
- 5.4.2.6
- UniProt
- P71447
- Ligands
- ALF, BG6, MG, NA
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-phosphoglucomutase (EC 5.4.2.6) | protein | 218 | 50% helix, 12% strand | P71447 |
Ligands and binding sites
- ALF · Tetrafluoroaluminate ion · ligand · chains A
- BG6 · 6-O-phosphono-beta-D-glucopyranose · sugar · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- NA · Sodium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.75 | 0.94 | 32 | ALF, MG, BG6 |
| 2 | 119 | 0.41 | 0.76 | 19 | EDO |
Compared structures
- 5OK2 · Structure of the D10N mutant of beta-phosphoglucomutase from Lactococcus lactis inhibited… · the same entry in another collection · chain A against A, TM-score 1.00
- P71447 · AlphaFold monomer V2.0 prediction for beta-phosphoglucomutase (P71447) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P71447
- Elsewhere: RCSB PDB 5OK2 · PDBe 5OK2 · UniProt P71447
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