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3hlm

X-ray diffraction
2.5Å resolution

Crystal Structure of Mouse Mitochondrial Aspartate Aminotransferase/Kynurenine Aminotransferase IV

Released:
Source organism: Mus musculus

Function and Biology Details

Reactions catalysed:
[L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate., L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate., L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate., L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.]
[L-kynurenine + 2-oxoglutarate = kynurenate + L-glutamate + H2O., L-kynurenine + 2-oxoglutarate = kynurenate + L-glutamate + H2O., L-kynurenine + 2-oxoglutarate = kynurenate + L-glutamate + H2O., L-kynurenine + 2-oxoglutarate = kynurenate + L-glutamate + H2O.]
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-138595 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 401 amino acids
Theoretical weight: 44.87 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P05202 (Residues: 30-430; Coverage: 93%)
Gene names: Got-2, Got2
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21212
Unit cell:
a: 284.322Å b: 76.792Å c: 87.416Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.181 0.234
Expression system: Escherichia coli