2CST
CRYSTAL STRUCTURE OF THE CLOSED FORM OF CHICKEN CYTOSOLIC ASPARTATE AMINOTRANSFERASE AT 1.9 ANGSTROMS RESOLUTION
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 | 0004609 | molecular_function | phosphatidylserine decarboxylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006107 | biological_process | oxaloacetate metabolic process |
| A | 0006114 | biological_process | glycerol biosynthetic process |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006531 | biological_process | aspartate metabolic process |
| A | 0006532 | biological_process | aspartate biosynthetic process |
| A | 0006533 | biological_process | aspartate catabolic process |
| A | 0006536 | biological_process | glutamate metabolic process |
| A | 0007219 | biological_process | Notch signaling pathway |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0019550 | biological_process | glutamate catabolic process to aspartate |
| A | 0019551 | biological_process | glutamate catabolic process to 2-oxoglutarate |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0032869 | biological_process | cellular response to insulin stimulus |
| A | 0047801 | molecular_function | L-cysteine transaminase activity |
| A | 0051384 | biological_process | response to glucocorticoid |
| A | 0055089 | biological_process | fatty acid homeostasis |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| B | 0004609 | molecular_function | phosphatidylserine decarboxylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| B | 0006107 | biological_process | oxaloacetate metabolic process |
| B | 0006114 | biological_process | glycerol biosynthetic process |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006531 | biological_process | aspartate metabolic process |
| B | 0006532 | biological_process | aspartate biosynthetic process |
| B | 0006533 | biological_process | aspartate catabolic process |
| B | 0006536 | biological_process | glutamate metabolic process |
| B | 0007219 | biological_process | Notch signaling pathway |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0019550 | biological_process | glutamate catabolic process to aspartate |
| B | 0019551 | biological_process | glutamate catabolic process to 2-oxoglutarate |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0032869 | biological_process | cellular response to insulin stimulus |
| B | 0047801 | molecular_function | L-cysteine transaminase activity |
| B | 0051384 | biological_process | response to glucocorticoid |
| B | 0055089 | biological_process | fatty acid homeostasis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 413 |
| Chain | Residue |
| A | GLY107 |
| A | GLY108 |
| A | THR109 |
| A | TRP140 |
| A | ASN194 |
| A | ASP222 |
| A | ALA224 |
| A | TYR225 |
| A | SER255 |
| A | SER257 |
| A | LYS258 |
| A | ARG266 |
| A | MAE414 |
| A | HOH416 |
| B | TYR70 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MAE A 414 |
| Chain | Residue |
| A | PHE18 |
| A | VAL37 |
| A | GLY38 |
| A | TRP140 |
| A | ASN194 |
| A | ARG386 |
| A | PLP413 |
| A | HOH416 |
| A | HOH423 |
| B | ARG292 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP B 413 |
| Chain | Residue |
| A | TYR70 |
| B | GLY107 |
| B | GLY108 |
| B | THR109 |
| B | TRP140 |
| B | ASN194 |
| B | ASP222 |
| B | ALA224 |
| B | TYR225 |
| B | SER255 |
| B | SER257 |
| B | LYS258 |
| B | ARG266 |
| B | MAE414 |
| B | HOH458 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MAE B 414 |
| Chain | Residue |
| A | ARG292 |
| B | VAL17 |
| B | PHE18 |
| B | VAL37 |
| B | GLY38 |
| B | TRP140 |
| B | ASN194 |
| B | ARG386 |
| B | PLP413 |
| B | HOH458 |
| B | HOH464 |
| site_id | ACT |
| Number of Residues | 24 |
| Details | THE ACTIVE SITE COMPRISES THE RESIDUES INTERACTING WITH COENZYME AND INHIBITOR. NOTE THAT RESIDUES TYR 70, ARG 292, SER 296, AND ASN 297 OF ONE SUBUNIT CONTRIBUTE TO THE ACTIVE SITE OF THE OTHER SUBUNIT IN THE DIMER. |
| Chain | Residue |
| A | VAL15 |
| A | THR109 |
| A | TRP140 |
| A | ASN194 |
| A | ASP222 |
| A | ALA224 |
| A | TYR225 |
| A | SER255 |
| A | LYS258 |
| A | ARG266 |
| B | ARG292 |
| A | VAL17 |
| B | SER296 |
| B | ASN297 |
| A | PHE360 |
| A | ARG386 |
| A | MAE414 |
| A | PHE18 |
| A | VAL37 |
| A | GLY38 |
| A | ALA39 |
| B | TYR70 |
| A | GLY107 |
| A | GLY108 |
| site_id | BCT |
| Number of Residues | 24 |
| Details | THE ACTIVE SITE COMPRISES THE RESIDUES INTERACTING WITH COENZYME AND INHIBITOR. NOTE THAT RESIDUES TYR 70, ARG 292, SER 296, AND ASN 297 OF ONE SUBUNIT CONTRIBUTE TO THE ACTIVE SITE OF THE OTHER SUBUNIT IN THE DIMER. |
| Chain | Residue |
| B | VAL15 |
| B | VAL17 |
| B | PHE18 |
| B | VAL37 |
| B | GLY38 |
| B | ALA39 |
| A | TYR70 |
| B | GLY107 |
| 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 | MAE414 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKnfGLyNERVG |
| Chain | Residue | Details |
| A | SER255-GLY268 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ALA39 | |
| A | GLU141 | |
| A | PRO195 | |
| A | ILE387 | |
| B | ALA39 | |
| B | GLU141 | |
| B | PRO195 | |
| B | ILE387 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:499525 |
| Chain | Residue | Details |
| A | ALA3 | |
| B | ALA3 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | ASN259 | |
| B | ASN259 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TRP140 | |
| A | ASP222 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TRP140 | |
| B | ASP222 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TRP140 | |
| A | ASP222 | |
| A | LYS258 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TRP140 | |
| B | ASP222 | |
| B | LYS258 |
