6jqo

Electron Microscopy
3.1Å resolution

Structure of PaaZ, a bifunctional enzyme in complex with NADP+ and CCoA

Released:

Function and Biology Details

Reactions catalysed:
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP(+) + H(2)O = 3-oxo-5,6-dehydrosuberyl-CoA + NADPH
2-oxepin-2(3H)-ylideneacetyl-CoA + H(2)O = 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein PaaZ Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 688 amino acids
Theoretical weight: 73.97 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P77455 (Residues: 2-681; Coverage: 100%)
Gene names: JW1382, b1387, maoC, paaZ, ydbN
Sequence domains:

Ligands and Environments


Cofactor: Ligand NAP 6 x NAP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.1Å
Relevant EMDB volumes: EMD-9876
Expression system: Escherichia coli BL21(DE3)