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Crystal structure of human liver 6-phosphofructo-2-KINASE/FRUCTOSE-2, 6-bisphosphatase
Analyse Crystal structure of human liver 6-phosphofructo-2-KINASE/FRUCTOSE-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K6M
- Type
- protein
- Length
- 864 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-biphosphatase 2- phosphatase
- EC
- 2.7.1.105, 3.1.3.46
- UniProt
- P16118
- Ligands
- AGS, PO4
- Pockets
- 7 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-biphosphatase 2- phosphatase (EC 2.7.1.105, 3.1.3.46) | protein | 432 | 43% helix, 16% strand | P16118 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 785 | 0.83 | 0.86 | 90 | AGS |
| 2 | 760 | 0.83 | 0.86 | 85 | AGS |
| 3 | 191 | 0.79 | 0.94 | 40 | PO4 |
| 4 | 182 | 0.79 | 0.94 | 42 | PO4 |
| 5 | 509 | 0.67 | 0.78 | 50 | empty |
Interfaces
1 interface between chains.
- A–B · 372 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1K6M · Crystal Structure of Human Liver 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase · the same entry in another collection · chain A against A, TM-score 1.00
- P16118 · 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 P16118
- Elsewhere: RCSB PDB 1K6M · PDBe 1K6M · UniProt P16118
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