Research workbench
Crystal Structure of Phosphofructokinase from Staphylococcus aureus in complex with ADP
Analyse Crystal Structure of Phosphofructokinase from Staphylococcus aureus in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XZA
- Type
- protein
- Length
- 322 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Staphylococcus aureus (strain NCTC 8325)
- Molecule
- ATP-dependent 6-phosphofructokinase
- EC
- 2.7.1.11
- UniProt
- Q2FXM8
- Ligands
- ADP
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent 6-phosphofructokinase (EC 2.7.1.11) | protein | 322 | 44% helix, 19% strand | Q2FXM8 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- FLC · Citrate anion · additive · 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 | 259 | 0.56 | 0.77 | 31 | ADP |
| 2 | 253 | 0.53 | 0.76 | 32 | empty |
Compared structures
- 5XZA · Crystal structure of phosphofructokinase from staphylococcus aureus in complex with ADP · the same entry in another collection · chain A against A, TM-score 1.00
- Q2FXM8 · AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase (Q2FXM8) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q2FXM8
- Elsewhere: RCSB PDB 5XZA · PDBe 5XZA · UniProt Q2FXM8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.