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alkyldihydroxyacetonephosphate synthase in P1
Analyse alkyldihydroxyacetonephosphate synthase in P1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UUV
- Type
- protein
- Length
- 2,065 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.99
- Source
- DICTYOSTELIUM DISCOIDEUM
- Molecule
- Alkyldihydroxyacetonephosphate synthase
- EC
- 2.5.1.26
- UniProt
- O96759
- Ligands
- FAD, PL3
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · resolution 1.99 · 4 distinct chains · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alkyldihydroxyacetonephosphate synthase (EC 2.5.1.26) | protein | 523 | 37% helix, 24% strand | O96759 |
| B | Alkyldihydroxyacetonephosphate synthase (EC 2.5.1.26) | protein | 523 | 37% helix, 24% strand | O96759 |
| C | Alkyldihydroxyacetonephosphate synthase (EC 2.5.1.26) | protein | 491 | 36% helix, 25% strand | O96759 |
| D | Alkyldihydroxyacetonephosphate synthase (EC 2.5.1.26) | protein | 528 | 37% helix, 24% strand | O96759 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- PL3 · Hexadecan-1-ol · ligand · 3 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 727 | 0.84 | 0.87 | 72 | FAD, PL3 |
| 2 | 691 | 0.84 | 0.87 | 67 | FAD, PL3 |
| 3 | 698 | 0.83 | 0.87 | 69 | FAD, PL3 |
| 4 | 861 | 0.82 | 0.84 | 79 | FAD |
| 5 | 1093 | 0.75 | 0.78 | 77 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1899 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1858 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 526 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 17 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 O96759
- Elsewhere: RCSB PDB 2UUV · PDBe 2UUV · UniProt O96759
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