Research workbench
Crystal structure of riboflavin kinase with ternary product complex
Analyse Crystal structure of riboflavin kinase with ternary product complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q9S
- Type
- protein
- Length
- 149 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein FLJ11149
- EC
- 2.7.1.26
- UniProt
- Q969G6
- Ligands
- ADP, FMN, MG
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein FLJ11149 (EC 2.7.1.26) | protein | 149 | 26% helix, 29% strand | Q969G6 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- FMN · Flavin mononucleotide · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 310 | 0.78 | 0.89 | 43 | MG, ADP, FMN |
| 2 | 66 | 0.32 | 0.75 | 17 | empty |
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 Q969G6
- Elsewhere: RCSB PDB 1Q9S · PDBe 1Q9S · UniProt Q969G6
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