Crystal structure of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).

Ligands and binding sites

• PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · 2 copies · chains A, B, C, D
• KYN · (2S)-2-amino-4-(2-aminophenyl)-4-oxobutanoic acid · ligand · chains A, B
• GOL · Glycerol · additive · 13 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Interfaces

4 interfaces between chains.

• A–B · 3301 Ų buried · 50 hydrogen bonds · protein-protein
• C–D · 3293 Ų buried · 52 hydrogen bonds · protein-protein
• A–C · 554 Ų buried · 2 hydrogen bonds · protein-protein
• B–D · 150 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 2 modified (cofactor).

Compared structures

• 3PD6 · Crystal structure of mouse mitochondrial aspartate aminotransferase, a newly identified… · the same entry in another collection · chain A against A, TM-score 1.00
• P05202 · AlphaFold monomer V2.0 prediction for aspartate aminotransferase, mitochondrial (P05202) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P05202
• Elsewhere: RCSB PDB 3PD6 · PDBe 3PD6 · UniProt P05202