Research workbench
Glucokinase in complex with an activator and glucose
Analyse Glucokinase in complex with an activator and glucose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VEV
- Type
- protein
- Length
- 450 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucokinase
- EC
- 2.7.1.2
- UniProt
- P35557
- Ligands
- 0H4, GLC, NA
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucokinase (EC 2.7.1.2) | protein | 450 | 46% helix, 20% strand | P35557 |
Ligands and binding sites
- 0H4 · (2S)-3-cyclopentyl-N-(5-methylpyridin-2-yl)-2-[2-oxo-4-(trifluoromethyl)pyridin-1(2H)-yl]propanamide · ligand · chains A
- GLC · alpha-D-glucopyranose · sugar · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 227 | 0.63 | 0.83 | 42 | GLC |
| 2 | 309 | 0.58 | 0.77 | 33 | 0H4 |
| 3 | 233 | 0.49 | 0.75 | 35 | empty |
| 4 | 55 | 0.33 | 0.78 | 15 | empty |
Compared structures
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 P35557
- Elsewhere: RCSB PDB 3VEV · PDBe 3VEV · UniProt P35557
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