Research workbench
Crystal structure of lpxk from aquifex aeolicus at 1.9 ångström resolution
Analyse Crystal structure of lpxk from aquifex aeolicus at 1.9 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EHX
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetraacyldisaccharide 4'-kinase
- EC
- 2.7.1.130
- UniProt
- O67572
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetraacyldisaccharide 4'-kinase (EC 2.7.1.130) | protein | 315 | 31% helix, 27% strand | O67572 |
Ligands and binding sites
- GOL · Glycerol · additive · 8 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 888 | 0.74 | 0.78 | 64 | GOL |
| 2 | 92 | 0.34 | 0.74 | 17 | EPE |
| 3 | 60 | 0.32 | 0.76 | 20 | empty |
Compared structures
- 4EHX · Crystal structure of LpxK from Aquifex aeolicus at 1.9 angstrom resolution · the same entry in another collection · chain A against A, TM-score 1.00
- O67572 · AlphaFold monomer V2.0 prediction for tetraacyldisaccharide 4'-kinase (O67572) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 O67572
- Elsewhere: RCSB PDB 4EHX · PDBe 4EHX · UniProt O67572
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