1YAA
ASPARTATE AMINOTRANSFERASE FROM SACCHAROMYCES CEREVISIAE CYTOPLASM
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 | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006531 | biological_process | aspartate metabolic process |
| A | 0006532 | biological_process | aspartate biosynthetic process |
| A | 0006536 | biological_process | glutamate metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0032938 | biological_process | negative regulation of translation in response to oxidative stress |
| A | 0043023 | molecular_function | ribosomal large subunit binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005829 | cellular_component | cytosol |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006531 | biological_process | aspartate metabolic process |
| B | 0006532 | biological_process | aspartate biosynthetic process |
| B | 0006536 | biological_process | glutamate metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0032938 | biological_process | negative regulation of translation in response to oxidative stress |
| B | 0043023 | molecular_function | ribosomal large subunit binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005777 | cellular_component | peroxisome |
| C | 0005829 | cellular_component | cytosol |
| C | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006531 | biological_process | aspartate metabolic process |
| C | 0006532 | biological_process | aspartate biosynthetic process |
| C | 0006536 | biological_process | glutamate metabolic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0032938 | biological_process | negative regulation of translation in response to oxidative stress |
| C | 0043023 | molecular_function | ribosomal large subunit binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005777 | cellular_component | peroxisome |
| D | 0005829 | cellular_component | cytosol |
| D | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006531 | biological_process | aspartate metabolic process |
| D | 0006532 | biological_process | aspartate biosynthetic process |
| D | 0006536 | biological_process | glutamate metabolic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0032938 | biological_process | negative regulation of translation in response to oxidative stress |
| D | 0043023 | molecular_function | ribosomal large subunit binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MAE A 901 |
| Chain | Residue |
| A | PHE18 |
| A | ILE37 |
| A | GLY38 |
| A | TRP140 |
| A | ASN194 |
| A | LYS258 |
| A | ARG386 |
| B | ARG292 |
| B | HOH907 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP A 905 |
| 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 | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MAE B 902 |
| Chain | Residue |
| A | TYR70 |
| A | ARG292 |
| B | LEU17 |
| B | PHE18 |
| B | GLY38 |
| B | TRP140 |
| B | ASN194 |
| B | LYS258 |
| B | ARG386 |
| B | PLP906 |
| B | HOH948 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 906 |
| Chain | Residue |
| A | TYR70 |
| B | SER107 |
| B | GLY108 |
| B | THR109 |
| B | TRP140 |
| B | ASN194 |
| B | ASP222 |
| B | ALA224 |
| B | TYR225 |
| B | SER255 |
| B | ALA257 |
| B | LYS258 |
| B | ARG266 |
| B | MAE902 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MAE C 903 |
| Chain | Residue |
| C | LEU17 |
| C | GLY38 |
| C | TRP140 |
| C | ASN194 |
| C | LYS258 |
| C | ARG386 |
| C | HOH948 |
| D | ARG292 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP C 907 |
| Chain | Residue |
| C | SER107 |
| C | GLY108 |
| C | THR109 |
| C | LEU112 |
| C | TRP140 |
| C | ASN194 |
| C | ASP222 |
| C | ALA224 |
| C | SER255 |
| C | ALA257 |
| C | LYS258 |
| C | ARG266 |
| C | HOH948 |
| D | TYR70 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MAE D 904 |
| Chain | Residue |
| C | ARG292 |
| D | LEU17 |
| D | PHE18 |
| D | GLY38 |
| D | TRP140 |
| D | ASN194 |
| D | ARG386 |
| D | HOH957 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP D 908 |
| Chain | Residue |
| C | TYR70 |
| D | SER107 |
| D | GLY108 |
| D | THR109 |
| D | TRP140 |
| D | ASN194 |
| D | ASP222 |
| D | ALA224 |
| D | TYR225 |
| D | SER255 |
| D | LYS258 |
| D | ARG266 |
| D | HOH957 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFAKnaGMyGERVG |
| Chain | Residue | Details |
| A | SER255-GLY268 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9655342 |
| Chain | Residue | Details |
| A | ALA39 | |
| C | ALA141 | |
| C | PRO195 | |
| C | ALA387 | |
| D | ALA39 | |
| D | ALA141 | |
| D | PRO195 | |
| D | ALA387 | |
| A | ALA141 | |
| A | PRO195 | |
| A | ALA387 | |
| B | ALA39 | |
| B | ALA141 | |
| B | PRO195 | |
| B | ALA387 | |
| C | ALA39 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:1859361, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | ALA3 | |
| B | ALA3 | |
| C | ALA3 | |
| D | ALA3 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:9655342 |
| Chain | Residue | Details |
| A | ASN259 | |
| B | ASN259 | |
| C | ASN259 | |
| D | ASN259 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358 |
| Chain | Residue | Details |
| A | ILE389 | |
| B | ILE389 | |
| C | ILE389 | |
| D | ILE389 |
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 | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | TRP140 | |
| C | ASP222 | |
| C | LYS258 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | TRP140 | |
| D | ASP222 | |
| D | LYS258 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TRP140 | |
| A | ASP222 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TRP140 | |
| B | ASP222 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | TRP140 | |
| C | ASP222 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | TRP140 | |
| D | ASP222 |
