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Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, and beryllium trifluoride, crystal form 2
Analyse Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WF9
- Type
- protein
- Length
- 221 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
- BEF, G6P, BG6, MG, NA
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-phosphoglucomutase (EC 5.4.2.6) | protein | 221 | 52% helix, 11% strand | P71447 |
Ligands and binding sites
- BEF · Beryllium trifluoride ion · ligand · chains A
- G6P · 6-O-phosphono-alpha-D-glucopyranose · sugar · chains A
- BG6 · 6-O-phosphono-beta-D-glucopyranose · sugar · chains A
- MG · Magnesium ion · metal · chains A
- NA · Sodium ion · metal · 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 | 200 | 0.68 | 0.86 | 43 | MG, G6P, BG6, BEF |
| 2 | 71 | 0.43 | 0.81 | 22 | empty |
Compared structures
- 2WF9 · Structure of Beta-Phosphoglucomutase inhibited with Glucose-6- phosphate, and Beryllium… · 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 0.94
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 2WF9 · PDBe 2WF9 · UniProt P71447
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