6kdf

X-ray diffraction
3.05Å resolution

Crystal structure of the alpha beta heterodimer of human IDH3 in APO form.

Released:

Function and Biology Details

Reaction catalysed:
Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-129150 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial Chains: A, B, E, G, I, K, M, O
Molecule details ›
Chains: A, B, E, G, I, K, M, O
Length: 341 amino acids
Theoretical weight: 36.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P50213 (Residues: 28-366; Coverage: 93%)
Gene name: IDH3A
Sequence domains: Isocitrate/isopropylmalate dehydrogenase
Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial Chains: C, D, F, H, J, L, N, P
Molecule details ›
Chains: C, D, F, H, J, L, N, P
Length: 356 amino acids
Theoretical weight: 39.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43837 (Residues: 35-374; Coverage: 88%)
Gene name: IDH3B
Sequence domains: Isocitrate/isopropylmalate dehydrogenase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: C2
Unit cell:
a: 208.913Å b: 170.434Å c: 208.094Å
α: 90° β: 103.43° γ: 90°
R-values:
R R work R free
0.18 0.177 0.227
Expression system: Escherichia coli