Research workbench
Crystal structure of the dihydroxyacetone kinase from E. COLI in complex with glyceraldehyde
Analyse Crystal structure of the dihydroxyacetone kinase from E. COLI in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UOE
- Type
- protein
- Length
- 672 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydroxyacetone kinase
- EC
- 2.7.1.29
- UniProt
- P76015
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dihydroxyacetone kinase (EC 2.7.1.29) | protein | 336 | 32% helix, 32% strand | P76015 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1171 | 0.82 | 0.83 | 111 | SO4 |
| 2 | 63 | 0.40 | 0.80 | 16 | empty |
| 3 | 54 | 0.37 | 0.80 | 16 | empty |
| 4 | 75 | 0.35 | 0.76 | 25 | empty |
| 5 | 69 | 0.33 | 0.75 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1276 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 1UOE · Crystal structure of the dihydroxyacetone kinase from E. coli in complex with… · the same entry in another collection · chain B against B, TM-score 1.00
- P76015 · AlphaFold monomer V2.0 prediction for pep-dependent dihydroxyacetone kinase… · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P76015
- Elsewhere: RCSB PDB 1UOE · PDBe 1UOE · UniProt P76015
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