Research workbench
E. COLI prpp synthetase
Analyse E. COLI prpp synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ASV
- Type
- protein
- Length
- 919 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribose-phosphate pyrophosphokinase
- EC
- 2.7.6.1
- UniProt
- P0A719
- Ligands
- PO4, CL
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribose-phosphate pyrophosphokinase (EC 2.7.6.1) | protein | 305 | 36% helix, 26% strand | P0A719 |
| B | Ribose-phosphate pyrophosphokinase (EC 2.7.6.1) | protein | 303 | 35% helix, 24% strand | P0A719 |
| C | Ribose-phosphate pyrophosphokinase (EC 2.7.6.1) | protein | 311 | 34% helix, 25% strand | P0A719 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 6 copies · chains A, B, C
- CL · Chloride ion · ion · 2 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1144 | 0.75 | 0.78 | 99 | PO4 |
| 2 | 193 | 0.51 | 0.77 | 34 | PO4 |
| 3 | 56 | 0.36 | 0.79 | 23 | empty |
| 4 | 97 | 0.36 | 0.75 | 18 | empty |
| 5 | 73 | 0.34 | 0.76 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2007 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 1872 Ų buried · 26 hydrogen bonds · protein-protein
- A–C · 356 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 P0A719
- Elsewhere: RCSB PDB 6ASV · PDBe 6ASV · UniProt P0A719
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