Research workbench
Crystal structure of phosphofructokinase from staphylococcus aureus in complex with adenylylimidodiphosphate, the ATP analogue
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
- 5XZ7
- Type
- protein
- Length
- 322 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent 6-phosphofructokinase
- EC
- 2.7.1.11
- UniProt
- Q2FXM8
- Ligands
- F6P
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent 6-phosphofructokinase (EC 2.7.1.11) | protein | 322 | 46% helix, 19% strand | Q2FXM8 |
Ligands and binding sites
- F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · chains A
- GOL · Glycerol · additive · 6 copies · chains A
- PEG · Di(hydroxyethyl)ether · 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 | 69 | 0.51 | 0.85 | 19 | GOL |
| 2 | 208 | 0.50 | 0.76 | 32 | GOL, F6P |
Compared structures
- 5XZ7 · Crystal Structure of Phosphofructokinase from Staphylococcus aureus in complex with… · 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 5XZ7 · PDBe 5XZ7 · UniProt Q2FXM8
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