Research workbench
Crystal structure of F181Q ubix in complex with FMN and dimethylallyl monophosphate
Analyse Crystal structure of F181Q ubix in complex with FMN and dimethylallyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QLI
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavin prenyltransferase ubix
- EC
- 2.5.1.129
- UniProt
- A0A072ZCW8
- Ligands
- 4LR, FNR, NA
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flavin prenyltransferase ubix (EC 2.5.1.129) | protein | 206 | 42% helix, 14% strand | A0A072ZCW8 |
Ligands and binding sites
- 4LR · Dimethylallyl monophosphate · ligand · chains A
- FNR · 1-deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydro-2H-benzo[g]pteridin-1-id-10(5H)-yl)-5-O-phosphonato-D-ribitol · ligand · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6QLI · Crystal structure of F181Q UbiX in complex with FMN and dimethylallyl monophosphate · 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 A0A072ZCW8
- Elsewhere: RCSB PDB 6QLI · PDBe 6QLI · UniProt A0A072ZCW8
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