Research workbench
Swine dUTPase in complex with alpha,beta-iminodUTP and magnesium ion
Analyse Swine dUTPase in complex with alpha,beta-iminodUTP and magnesium ion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LJJ
- Type
- protein
- Length
- 150 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.89
- Source
- Sus scrofa
- Molecule
- Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial isoform 1
- UniProt
- A0A480PG39
- Ligands
- DUP, MG
Structure
x-ray diffraction · resolution 1.89 · 1 distinct chain · 10% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial isoform 1 | protein | 150 | 10% helix, 36% strand | A0A480PG39 |
Ligands and binding sites
- DUP · 2'-deoxyuridine 5'-alpha,beta-imido-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6LJJ · Swine dutpase in complex with ALPHA,BETA-iminodutp and magnesium ion · 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 A0A480PG39
- Elsewhere: RCSB PDB 6LJJ · PDBe 6LJJ · UniProt A0A480PG39
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