Function and Biology Details
Reaction catalysed:
Nucleoside triphosphate + gentamicin = diphosphate + 2''-nucleotidylgentamicin
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
2''-aminoglycoside nucleotidyltransferase (preferred)
PDBe Complex ID:
PDB-CPX-142393 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2''-aminoglycoside nucleotidyltransferase
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 20.96 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Aminoglycoside-2''-adenylyltransferase
Structure domains: Beta Polymerase; domain 2
Length: 185 amino acids
Theoretical weight: 20.96 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P0AE05 (Residues: 1-177; Coverage: 100%)
Sequence domains: Aminoglycoside-2''-adenylyltransferase
Structure domains: Beta Polymerase; domain 2
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
81%
Refinement method:
torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)
