Research workbench
Structural and catalytic analysis of two diverse uridine phosphorylases in the oomycete phytophthora capsici.
Analyse Structural and catalytic analysis of two diverse uridine phosphorylases in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6K5H
- Type
- protein
- Length
- 1,148 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A410UCT3
- Ligands
- URA, R1P
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 287 | — | A0A410UCT3 |
| B | — | protein | 286 | — | A0A410UCT3 |
| C | — | protein | 287 | — | A0A410UCT3 |
| D | — | protein | 288 | — | A0A410UCT3 |
Ligands and binding sites
- URA · Uracil · ligand · 4 copies · chains A, B, C, D
- R1P · 1-O-phosphono-alpha-D-ribofuranose · ligand · 4 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6K5H · Structural and catalytic analysis of two diverse uridine phosphorylases in the oomycete… · 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 A0A410UCT3
- Elsewhere: RCSB PDB 6K5H · PDBe 6K5H · UniProt A0A410UCT3
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