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Structure of S. aureus undecaprenyl diphosphate synthase in complex with FSPP and sulfate
Analyse Structure of S. aureus undecaprenyl diphosphate synthase in complex with FSPP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U82
- Type
- protein
- Length
- 236 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.66
- Source
- Staphylococcus aureus
- Molecule
- Isoprenyl transferase
- EC
- 2.5.1.-
- UniProt
- P60477
- Ligands
- FPS, MG, SO4
- Pockets
- 1 · best druggability 0.77
Structure
x-ray diffraction · resolution 1.66 · 1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoprenyl transferase (EC 2.5.1.-) | protein | 236 | 49% helix, 14% strand | P60477 |
Ligands and binding sites
- FPS · S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl] trihydrogen thiodiphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 285 | 0.77 | 0.89 | 37 | MG, FPS, SO4 |
Compared structures
- 4U82 · Structure of S. aureus undecaprenyl diphosphate synthase in complex with fspp and sulfate · the same entry in another collection · chain A against A, TM-score 1.00
- P60477 · AlphaFold monomer V2.0 prediction for isoprenyl transferase (P60477) · 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 P60477
- Elsewhere: RCSB PDB 4U82 · PDBe 4U82 · UniProt P60477
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