Research workbench
Crystal structure of purine nucleoside phosphorylase from streptococcus agalactiae 2603V/R, nysgrc target 030935
Analyse Crystal structure of purine nucleoside phosphorylase from streptococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TYM
- Type
- protein
- Length
- 235 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Purine nucleoside phosphorylase deod-type
- EC
- 2.4.2.1
- UniProt
- S9I310
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Purine nucleoside phosphorylase deod-type (EC 2.4.2.1) | protein | 235 | 37% helix, 29% strand | S9I310 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.58 | 0.77 | 41 | SO4 |
| 2 | 66 | 0.32 | 0.75 | 13 | empty |
Modifications
Observed in the structure: 12 modified (engineered, oxidation).
Compared structures
- 4TYM · Crystal structure of purine nucleoside phosphorylase from Streptococcus agalactiae… · 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 S9I310
- Elsewhere: RCSB PDB 4TYM · PDBe 4TYM · UniProt S9I310
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.