MolNFT v1 · #118136 · protein
Crystal structure of apo hypoxanthine-guanine phosphoribosyltransferase from legionella pneumophila
5ESW · PURINE/PYRIMIDINE phosphoribosyltransferase: “Crystal structure of apo hypoxanthine-guanine phosphoribosyltransferase from legionella pneumophila”. X-ray diffraction, 1 ligand (PO4), 5 pockets (best druggability 0.64). MolNFT v1…
- PDB
- 5ESW
- Type
- protein
- Length
- 379 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PURINE/PYRIMIDINE phosphoribosyltransferase
- EC
- 2.4.2.8
- UniProt
- Q5ZVC1
- Ligands
- PO4
- Pockets
- 5 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PURINE/PYRIMIDINE phosphoribosyltransferase (EC 2.4.2.8) | protein | 190 | 28% helix, 30% strand | Q5ZVC1 |
| B | PURINE/PYRIMIDINE phosphoribosyltransferase (EC 2.4.2.8) | protein | 189 | 30% helix, 30% strand | Q5ZVC1 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 479 | 0.64 | 0.76 | 50 | empty |
| 2 | 380 | 0.59 | 0.76 | 33 | empty |
| 3 | 56 | 0.45 | 0.84 | 19 | empty |
| 4 | 60 | 0.43 | 0.82 | 19 | empty |
| 5 | 90 | 0.35 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1474 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 5ESW · Crystal structure of Apo hypoxanthine-guanine phosphoribosyltransferase from Legionella… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5ZVC1
- Elsewhere: RCSB PDB 5ESW · PDBe 5ESW · UniProt Q5ZVC1
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