Research workbench
6-phosphofructo-2-KINASE/FRUCTOSE-2,6-bisphosphatase bifunctional enzyme complexed with ATP-G-S and phosphate
Analyse 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-bisphosphatase bifunctional enzyme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BIF
- Type
- protein
- Length
- 432 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 6-phosphofructo-2-kinase/ fructose-2,6-bisphosphatase
- EC
- 2.7.1.105, 3.1.3.46
- UniProt
- P25114
- Ligands
- AGS, MG, PO4
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 6-phosphofructo-2-kinase/ fructose-2,6-bisphosphatase (EC 2.7.1.105, 3.1.3.46) | protein | 432 | 44% helix, 16% strand | P25114 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 770 | 0.83 | 0.86 | 94 | MG, AGS |
| 2 | 158 | 0.79 | 0.95 | 35 | PO4 |
Compared structures
- 1BIF · 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-bisphosphatase bifunctional enzyme complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P25114 · AlphaFold monomer V2.0 prediction for 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-bisphosphatase… · a predicted model of the same protein · chain A 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 P25114
- Elsewhere: RCSB PDB 1BIF · PDBe 1BIF · UniProt P25114
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