Function and Biology Details
Reaction catalysed:
L-gulonate + NAD(+) = 3-dehydro-L-gulonate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- 6-phosphogluconate dehydrogenase, domain 2
- 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
- 3-hydroxyacyl-CoA dehydrogenase, C-terminal
- 3-hydroxyacyl-CoA dehydrogenase, conserved site
- 3-hydroxyacyl-CoA dehydrogenase, NAD binding
- NAD(P)-binding domain superfamily
- 3-hydroxyacyl-CoA dehydrogenase
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Lambda-crystallin (preferred)
PDBe Complex ID:
PDB-CPX-147069 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lambda-crystallin
Molecule details ›
Chain: A
Length: 319 amino acids
Theoretical weight: 35.25 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 319 amino acids
Theoretical weight: 35.25 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
- Canonical:
P14755 (Residues: 1-319; Coverage: 100%)
Sequence domains:
- 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain
- 3-hydroxyacyl-CoA dehydrogenase, C-terminal domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SPRING-8 BEAMLINE BL26B1
Spacegroup:
C2
Expression system: Escherichia coli
