MolNFT v1 · #63823 · protein
Crystal structure of the his-tagged H232R mutant of glycerol kinase from enterococcus casseliflavus with glycerol
3FLC: “Crystal structure of the his-tagged H232R mutant of glycerol kinase from enterococcus casseliflavus with…”. X-ray diffraction, 1 ligand (SO4), 12 pockets (best druggability 0.76). MolNFT v1 #63823 on GenesisL1: 3D structure, binding…
- PDB
- 3FLC
- Type
- protein
- Length
- 991 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycerol kinase
- EC
- 2.7.1.30
- UniProt
- O34153
- Ligands
- SO4
- Pockets
- 12 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| O | Glycerol kinase (EC 2.7.1.30) | protein | 495 | 37% helix, 25% strand | O34153 |
| X | Glycerol kinase (EC 2.7.1.30) | protein | 496 | 38% helix, 25% strand | O34153 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 383 | 0.76 | 0.86 | 47 | GOL, SO4 |
| 2 | 478 | 0.75 | 0.83 | 49 | GOL, SO4 |
| 3 | 135 | 0.59 | 0.84 | 23 | empty |
| 4 | 69 | 0.57 | 0.88 | 20 | empty |
| 5 | 276 | 0.56 | 0.77 | 42 | empty |
Interfaces
1 interface between chains.
- O–X · 486 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3FLC · Crystal structure of the His-tagged H232R mutant of glycerol kinase from Enterococcus… · the same entry in another collection · chain O against O, TM-score 1.00
- O34153 · AlphaFold monomer V2.0 prediction for glycerol kinase (O34153) · a predicted model of the same protein · chain X 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 O34153
- Elsewhere: RCSB PDB 3FLC · PDBe 3FLC · UniProt O34153
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