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Phage dutpases control transfer of virulence genes by a proto- oncogenic G protein-like mechanism. (staphylococcus bacteriophage 80ALPHA dutpase D81A mutant with dupnhpp).
Analyse Phage dutpases control transfer of virulence genes by a proto- oncogenic G… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZF0
- Type
- protein
- Length
- 149 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dutpase
- EC
- 3.6.1.23
- UniProt
- A4ZF98
- Ligands
- DUP, NI
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dutpase (EC 3.6.1.23) | protein | 149 | 4% helix, 40% strand | A4ZF98 |
Ligands and binding sites
- DUP · 2'-deoxyuridine 5'-alpha,beta-imido-triphosphate · ligand · chains A
- NI · Nickel (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3ZF0 · Phage dUTPases control transfer of virulence genes by a proto-oncogenic G protein-like… · 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 3ZF0 · PDBe 3ZF0 · UniProt A4ZF98
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