Research workbench
X-ray structure of the complex pyrimidine-nucleoside phosphorylase from bacillus subtilis at 1.88 a
Analyse X-ray structure of the complex pyrimidine-nucleoside phosphorylase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OLN
- Type
- protein
- Length
- 867 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P39142
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 433 | — | P39142 |
| B | — | protein | 434 | — | P39142 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains B
- IMD · Imidazole · additive · 3 copies · chains A, B
- EDO · 1,2-ethanediol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OLN · X-Ray Structure of the Complex Pyrimidine-nucleoside phosphorylase from Bacillus subtilis… · the same entry in another collection · chain A against A, TM-score 1.00
- P39142 · AlphaFold monomer V2.0 prediction for pyrimidine-nucleoside phosphorylase (P39142) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P39142
- Elsewhere: RCSB PDB 5OLN · PDBe 5OLN · UniProt P39142
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