› 5kvq

X-ray diffraction
1.45Å resolution

NADP+ bound structure of Irp3, a Thiazolinyl Imine Reductase from Yersinia enterocolitica

Released:
DOI: 10.2210/pdb5kvq/pdb
PDB 5kvq coloured by chain and viewed from the front.
PDB 5kvq coloured by chain and viewed from the side.
PDB 5kvq coloured by chain and viewed from the top.
Source organism: Yersinia enterocolitica
Primary publication:
Holo Structure and Steady State Kinetics of the Thiazolinyl Imine Reductases for Siderophore Biosynthesis.
Meneely KM, Ronnebaum TA, Riley AP, Prisinzano TE, Lamb AL
Biochemistry (2016)
PMID: 27601130

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gfo/Idh/MocA-like oxidoreductase N-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 385 amino acids
Theoretical weight: 42.93 KDa
Source organism: Yersinia enterocolitica
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O54512 (Residues: 1-365; Coverage: 100%)
Gene name: irp3
Sequence domains: Oxidoreductase family, NAD-binding Rossmann fold
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand EDO 2 x EDO
Ligand NAP 2 x NAP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21
Unit cell:
a: 41.444Å b: 148.506Å c: 65.006Å
α: 90° β: 95.62° γ: 90°
R-values:
R R work R free
0.16 0.159 0.179
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study.
Ronnebaum et al. (2018)
2 more

1 mention without citation

Holo Structure and Steady State Kinetics of the Thiazolinyl Imine Reductases for Siderophore Biosynthesis.
Meneely et al. (2016)