Research workbench
Full length asfv dutpase in complex with ALPHA,BETA-iminodutp and magnesium ion
Analyse Full length asfv 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
- 6LJ3
- Type
- protein
- Length
- 449 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A2X0SE53
- Ligands
- DUP, MG
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 164 | — | A0A2X0SE53 |
| B | — | protein | 145 | — | A0A2X0SE53 |
| C | — | protein | 140 | — | A0A2X0SE53 |
Ligands and binding sites
- DUP · 2'-deoxyuridine 5'-alpha,beta-imido-triphosphate · ligand · 3 copies · chains A, C, B
- MG · Magnesium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6LJ3 · full length ASFV 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 A0A2X0SE53
- Elsewhere: RCSB PDB 6LJ3 · PDBe 6LJ3 · UniProt A0A2X0SE53
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