1TAT
CRYSTALLINE MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE EXISTS IN ONLY TWO CONFORMATIONS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006531 | biological_process | aspartate metabolic process |
| A | 0006533 | biological_process | L-aspartate catabolic process |
| A | 0006536 | biological_process | glutamate metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006531 | biological_process | aspartate metabolic process |
| B | 0006533 | biological_process | L-aspartate catabolic process |
| B | 0006536 | biological_process | glutamate metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP A 411 |
| Chain | Residue |
| A | SER107 |
| A | GLY108 |
| A | THR109 |
| A | TRP140 |
| A | ASN194 |
| A | ASP222 |
| A | ALA224 |
| A | TYR225 |
| A | SER255 |
| A | ALA257 |
| A | LYS258 |
| A | ARG266 |
| B | TYR70 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP B 411 |
| Chain | Residue |
| A | TYR70 |
| B | SER107 |
| B | GLY108 |
| B | THR109 |
| B | TRP140 |
| B | ASN194 |
| B | ASP222 |
| B | ALA224 |
| B | TYR225 |
| B | SER255 |
| B | LYS258 |
| B | ARG266 |
| site_id | ACT |
| Number of Residues | 24 |
| Details | RESIDUES INTERACTING WITH THE COENZYME PLP |
| Chain | Residue |
| A | ASP15 |
| A | THR109 |
| A | TRP140 |
| A | ASN194 |
| A | ASP222 |
| A | ALA224 |
| A | TYR225 |
| A | SER255 |
| A | LYS258 |
| A | ARG266 |
| B | ARG292 |
| A | ILE17 |
| B | SER296 |
| B | ASN297 |
| A | PHE360 |
| A | ARG386 |
| A | PLP411 |
| A | LEU18 |
| A | VAL37 |
| A | GLY38 |
| A | ALA39 |
| B | TYR70 |
| A | SER107 |
| A | GLY108 |
| site_id | BCT |
| Number of Residues | 24 |
| Details | RESIDUES INTERACTING WITH THE COENZYME PLP |
| Chain | Residue |
| B | ASP15 |
| B | ILE17 |
| B | LEU18 |
| B | VAL37 |
| B | GLY38 |
| B | ALA39 |
| A | TYR70 |
| B | SER107 |
| B | GLY108 |
| B | THR109 |
| B | TRP140 |
| B | ASN194 |
| B | ASP222 |
| B | ALA224 |
| B | TYR225 |
| B | SER255 |
| B | LYS258 |
| B | ARG266 |
| A | ARG292 |
| A | SER296 |
| A | ASN297 |
| B | PHE360 |
| B | ARG386 |
| B | PLP411 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYAKnmGLyGERAG |
| Chain | Residue | Details |
| A | SER255-GLY268 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TRP140 | |
| A | ASP222 | |
| A | LYS258 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TRP140 | |
| B | ASP222 | |
| B | LYS258 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TRP140 | |
| A | ASP222 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TRP140 | |
| B | ASP222 |
