MolNFT v1 · #155116 · protein
The ishigamide KETOSYNTHASE/CHAIN length factor
6KXF: “The ishigamide KETOSYNTHASE/CHAIN length factor”. X-ray diffraction, 1 ligand (DYF). MolNFT v1 #155116 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6KXF
- Type
- protein
- Length
- 836 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1Y1BW67, A0A1Y1BW66, A0A1Y1BWQ0
- Ligands
- DYF
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 403 | — | A0A1Y1BW67 |
| B | — | protein | 360 | — | A0A1Y1BW66 |
| C | — | protein | 73 | — | A0A1Y1BWQ0 |
Ligands and binding sites
- DYF · [(3~{R})-2,2-dimethyl-4-[[3-[2-[[(~{E})-oct-2-enoyl]amino]ethylamino]-3-oxidanylidene-propyl]amino]-3-oxidanyl-4-oxidanylidene-butyl] dihydrogen phosphate · ligand · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6KXF · 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
- Every structure of UniProt A0A1Y1BWQ0
- Elsewhere: RCSB PDB 6KXF · PDBe 6KXF · UniProt A0A1Y1BW67 · UniProt A0A1Y1BW66 · UniProt A0A1Y1BWQ0
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