Research workbench
Twist and induce: dissecting the link between the enzymatic activity and the sapi inducing capacity of the phage 80 dutpase. D95E mutant from dutpase 80ALPHA phage.
Analyse Twist and induce: dissecting the link between the enzymatic activity and the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NZ2
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dutpase
- UniProt
- A4ZF98
- Ligands
- DUP, MG
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dutpase | protein | 155 | 4% helix, 39% strand | A4ZF98 |
Ligands and binding sites
- DUP · 2'-deoxyuridine 5'-alpha,beta-imido-triphosphate · ligand · chains A
- MG · Magnesium ion · metal
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NZ2 · Twist and induce: Dissecting the link between the enzymatic activity and the SaPI… · 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 A4ZF98
- Elsewhere: RCSB PDB 5NZ2 · PDBe 5NZ2 · UniProt A4ZF98
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