Research workbench
The ishigamide KETOSYNTHASE/CHAIN length factor
Analyse The ishigamide KETOSYNTHASE/CHAIN length factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KXE
- Type
- protein
- Length
- 759 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ketosynthase
- UniProt
- A0A1Y1BW67, A0A1Y1BW66
- Ligands
- PO4
- Pockets
- 9 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ketosynthase | protein | 401 | 39% helix, 23% strand | A0A1Y1BW67 |
| B | Ketosynthase | protein | 358 | 42% helix, 22% strand | A0A1Y1BW66 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains B
- PPI · Propanoic acid · additive · chains A, B
- ACT · Acetate ion · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.71 | 0.96 | 18 | PPI |
| 2 | 143 | 0.65 | 0.87 | 21 | empty |
| 3 | 277 | 0.64 | 0.82 | 46 | empty |
| 4 | 128 | 0.47 | 0.78 | 26 | empty |
| 5 | 96 | 0.47 | 0.80 | 20 | EDO |
Interfaces
1 interface between chains.
- A–B · 3186 Ų buried · 50 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 6KXE · The ishigamide ketosynthase/chain length factor · the same entry in another collection · 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 A0A1Y1BW67
- Every structure of UniProt A0A1Y1BW66
- Elsewhere: RCSB PDB 6KXE · PDBe 6KXE · UniProt A0A1Y1BW67 · UniProt A0A1Y1BW66
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