Research workbench
Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase in complex with zinc ions
Analyse Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K4P
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- EC
- 5.4.99.-
- UniProt
- Q8TG90
- Ligands
- ZN, SO4
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3,4-dihydroxy-2-butanone 4-phosphate synthase (EC 5.4.99.-) | protein | 216 | 37% helix, 25% strand | Q8TG90 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.45 | 0.82 | 17 | SO4, ZN |
| 2 | 52 | 0.30 | 0.76 | 18 | empty |
Compared structures
- 1K4P · Crystal Structure of 3,4-dihydroxy-2-buta 4-phosphate synthase in complex with zinc ions · the same entry in another collection · chain A against A, TM-score 1.00
- Q8TG90 · AlphaFold monomer V2.0 prediction for 3,4-dihydroxy-2-butanone 4-phosphate synthase… · a predicted model of the same protein · chain A 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 Q8TG90
- Elsewhere: RCSB PDB 1K4P · PDBe 1K4P · UniProt Q8TG90
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