Research workbench
Human PFKFB3 in complex with an indole inhibitor 1
Analyse Human PFKFB3 in complex with an indole inhibitor 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AJV
- Type
- protein
- Length
- 435 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human PFKFB3
- EC
- 2.7.1.105, 3.1.3.46
- UniProt
- Q16875
- Ligands
- 8R2, FDP, PO4
- Pockets
- 3 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Human PFKFB3 (EC 2.7.1.105, 3.1.3.46) | protein | 435 | 43% helix, 18% strand | Q16875 |
Ligands and binding sites
- 8R2 · (2S)-2-amino-N-[4-[(2-amino-3-cyano-1H-indol-5-yl)oxy]phenyl]-3-hydroxy-propanamide · ligand · chains B
- FDP · 2,6-di-O-phosphono-beta-D-fructofuranose · ligand · chains B
- PO4 · Phosphate ion · ion · 3 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 779 | 0.81 | 0.84 | 82 | PO4, 8R2 |
| 2 | 198 | 0.73 | 0.89 | 35 | FDP |
| 3 | 51 | 0.33 | 0.78 | 13 | empty |
Compared structures
- 5AJV · Human PFKFB3 in complex with an indole inhibitor 1 · the same entry in another collection · chain B against B, TM-score 1.00
- Q16875 · AlphaFold monomer V2.0 prediction for 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-bisphosphatase… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q16875
- Elsewhere: RCSB PDB 5AJV · PDBe 5AJV · UniProt Q16875
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