MolNFT v1 · #2164 · protein
Crystal structure of the complex between escherichia COLI glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate.
1BO5 · Protein (glycerol kinase): “Crystal structure of the complex between escherichia COLI glycerol kinase and the allosteric regulator…”. X-ray diffraction, 1 ligand (FBP), 7 pockets (best druggability 0.69). MolNFT v1 #2164 on…
- PDB
- 1BO5
- Type
- protein
- Length
- 996 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (glycerol kinase)
- EC
- 2.7.1.30
- UniProt
- P0A6F3
- Ligands
- FBP
- Pockets
- 7 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| O, Z | Protein (glycerol kinase) (EC 2.7.1.30) | protein | 498 | 35% helix, 24% strand | P0A6F3 |
Ligands and binding sites
- FBP · 1,6-di-O-phosphono-beta-D-fructofuranose · ligand · chains O
- GOL · Glycerol · additive · 2 copies · chains O, Z
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 394 | 0.69 | 0.81 | 44 | GOL |
| 2 | 393 | 0.68 | 0.81 | 43 | GOL |
| 3 | 191 | 0.56 | 0.79 | 26 | empty |
| 4 | 186 | 0.54 | 0.79 | 24 | empty |
| 5 | 61 | 0.31 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- O–Z · 129 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1BO5 · Crystal structure of the complex between escherichia COLI glycerol kinase and the… · the same entry in another collection · chain Z against Z, TM-score 1.00
- P0A6F3 · AlphaFold monomer V2.0 prediction for glycerol kinase (P0A6F3) · a predicted model of the same protein · chain O 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 P0A6F3
- Elsewhere: RCSB PDB 1BO5 · PDBe 1BO5 · UniProt P0A6F3
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