› 5kmq

X-ray diffraction
2.7Å resolution

The structure of I379E variant of type II NADH dehydrogenase from Caldalkalibacillus thermarum

Released:
DOI: 10.2210/pdb5kmq/pdb
PDB entry 5kmq coloured by chain, front view.
PDB entry 5kmq coloured by chain, side view.
PDB entry 5kmq coloured by chain, top view.
Source organism: Caldalkalibacillus thermarum TA2.A1
Primary publication:
The mechanism of catalysis by type-II NADH:quinone oxidoreductases.
Blaza JN, Bridges HR, Aragão D, Dunn EA, Heikal A, Cook GM, Nakatani Y, Hirst J
Sci Rep 7 40165 (2017)
PMID: 28067272

Function and Biology Details

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-123583 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD/NAD(P)-binding domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 405 amino acids
Theoretical weight: 44.59 KDa
Source organism: Caldalkalibacillus thermarum TA2.A1
Expression system: Escherichia coli
UniProt:
  • Canonical: F5L3B8 (Residues: 1-399; Coverage: 100%)
Gene names: CathTA2_0279, HUR95_15605
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments

1 bound ligand:
Ligand FAD 4 x FAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21
Unit cell:
a: 72.383Å b: 114.366Å c: 130.462Å
α: 90° β: 92.04° γ: 90°
R-values:
R R work R free
0.225 0.223 0.269
Expression system: Escherichia coli

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Citations

7 review citations

Recent advances and perspectives in the design and development of polymyxins.
Rabanal et al. (2017)
6 more

1 mention without citation

The mechanism of catalysis by type-II NADH:quinone oxidoreductases.
Blaza et al. (2017)