› 6cbn

X-ray diffraction
1.35Å resolution

x-ray structure of NeoB from streptomyces fradiae in complex with PLP and neomycin (as the external aldimine) at pH 7.5

Released:
DOI: 10.2210/pdb6cbn/pdb
PDB entry 6cbn coloured by chain, front view.
PDB entry 6cbn coloured by chain, side view.
PDB entry 6cbn coloured by chain, top view.
Source organism: Streptomyces fradiae
Primary publication:
The three-dimensional structure of NeoB: An aminotransferase involved in the biosynthesis of neomycin.
Dow GT, Thoden JB, Holden HM
Protein Sci 27 945-956 (2018)
PMID: 29516565

Function and Biology Details

Reactions catalysed: 
Neamine + 2-oxoglutarate = 6'-dehydroparomamine + L-glutamate
Neomycin C + 2-oxoglutarate = 6'''-deamino-6'''-oxoneomycin C + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176119 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neamine transaminase NeoN Chains: A, B
Molecule details ›
Chains: A, B
Length: 438 amino acids
Theoretical weight: 47.16 KDa
Source organism: Streptomyces fradiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q53U08 (Residues: 1-416; Coverage: 100%)
Gene names: neo18, neoB, neoN
Sequence domains: Aminotransferase class-III

Ligands and Environments

2 bound ligands:
Ligand OZY 2 x OZY
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 59.255Å b: 109.576Å c: 70.443Å
α: 90° β: 110.5° γ: 90°
R-values:
R R work R free
0.173 0.172 0.197
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Complete reconstitution of the diverse pathways of gentamicin B biosynthesis.
Ban et al. (2019)
2 more

1 mention without citation

The three-dimensional structure of NeoB: An aminotransferase involved in the biosynthesis of neomycin.
Dow et al. (2018)