› 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 entry 5kvq coloured by chain, front view.
PDB entry 5kvq coloured by chain, side view.
PDB entry 5kvq coloured by chain, top view.
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 55 5423-33 (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)
Assembly name:
PDBe Complex ID:
PDB-CPX-129500 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Irp3 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:
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

4 review citations

Imine reductases (IREDs).
Mangas-Sanchez et al. (2017)
3 more

2 mentions without citation

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