Research workbench
Crystal structure of uridine phosphorylase from vibrio fischeri ES114, nysgrc target 29520.
Analyse Crystal structure of uridine phosphorylase from vibrio fischeri ES114, nysgrc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LNH
- Type
- protein
- Length
- 239 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uridine phosphorylase
- EC
- 2.4.2.3
- UniProt
- Q5E046
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uridine phosphorylase (EC 2.4.2.3) | protein | 239 | 35% helix, 30% strand | Q5E046 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.47 | 0.76 | 27 | SO4 |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 4LNH · Crystal structure of uridine phosphorylase from Vibrio fischeri ES114, NYSGRC Target… · 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 Q5E046
- Elsewhere: RCSB PDB 4LNH · PDBe 4LNH · UniProt Q5E046
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.