Research workbench
Human glucokinase in complex with a synthetic activator
Analyse Human glucokinase in complex with a synthetic activator in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H1V
- Type
- protein
- Length
- 446 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
- TK1, GLC, NA
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Glucokinase (EC 2.7.1.2) | protein | 446 | 41% helix, 21% strand | P35557 |
Ligands and binding sites
- TK1 · 1-({5-[4-(methylsulfonyl)phenoxy]-2-pyridin-2-yl-1H-benzimidazol-6-yl}methyl)pyrrolidine-2,5-dione · ligand · chains X
- GLC · alpha-D-glucopyranose · sugar · chains X
- NA · Sodium ion · metal · chains X
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 | 328 | 0.70 | 0.83 | 31 | TK1 |
| 2 | 307 | 0.60 | 0.79 | 46 | GLC |
| 3 | 114 | 0.40 | 0.75 | 25 | 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 3H1V · PDBe 3H1V · UniProt P35557
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