1BKG
ASPARTATE AMINOTRANSFERASE FROM THERMUS THERMOPHILUS WITH MALEATE
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 | 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 | 0033853 | molecular_function | aspartate-prephenate aminotransferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0033853 | molecular_function | aspartate-prephenate aminotransferase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| 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 | 0033853 | molecular_function | aspartate-prephenate aminotransferase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| 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 | 0033853 | molecular_function | aspartate-prephenate aminotransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PMP A 413 |
| Chain | Residue |
| A | GLY99 |
| A | ARG242 |
| A | MAE414 |
| A | HOH502 |
| B | TYR64 |
| B | HOH503 |
| A | GLY100 |
| A | LYS101 |
| A | ASN171 |
| A | ASN175 |
| A | ASP203 |
| A | ILE205 |
| A | TYR206 |
| A | LYS234 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MAE A 414 |
| Chain | Residue |
| A | THR16 |
| A | LYS101 |
| A | TRP125 |
| A | ASN175 |
| A | ARG361 |
| A | PMP413 |
| A | HOH503 |
| B | HOH503 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PMP B 413 |
| Chain | Residue |
| A | TYR64 |
| A | HOH555 |
| B | GLY99 |
| B | GLY100 |
| B | LYS101 |
| B | ASN171 |
| B | ASN175 |
| B | ASP203 |
| B | ILE205 |
| B | TYR206 |
| B | LYS234 |
| B | ARG242 |
| B | MAE414 |
| B | HOH502 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MAE B 414 |
| Chain | Residue |
| A | HOH555 |
| B | THR16 |
| B | LYS101 |
| B | TRP125 |
| B | ASN175 |
| B | ARG361 |
| B | PMP413 |
| B | HOH504 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PMP C 413 |
| Chain | Residue |
| C | GLY99 |
| C | GLY100 |
| C | LYS101 |
| C | TRP125 |
| C | ASN171 |
| C | ASN175 |
| C | ASP203 |
| C | ILE205 |
| C | TYR206 |
| C | LYS234 |
| C | ARG242 |
| C | MAE414 |
| C | HOH502 |
| D | TYR64 |
| D | HOH516 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MAE C 414 |
| Chain | Residue |
| C | THR16 |
| C | LYS101 |
| C | TRP125 |
| C | ASN175 |
| C | ARG361 |
| C | PMP413 |
| C | HOH504 |
| D | HOH516 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PMP D 413 |
| Chain | Residue |
| C | TYR64 |
| C | HOH503 |
| D | GLY99 |
| D | GLY100 |
| D | LYS101 |
| D | ASN171 |
| D | ASN175 |
| D | ASP203 |
| D | ILE205 |
| D | TYR206 |
| D | LYS234 |
| D | ARG242 |
| D | MAE414 |
| D | HOH531 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MAE D 414 |
| Chain | Residue |
| D | THR16 |
| D | LYS101 |
| D | TRP125 |
| D | ASN175 |
| D | ARG361 |
| D | PMP413 |
| D | HOH532 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GAAKafAMtGWRIG |
| Chain | Residue | Details |
| A | GLY231-GLY244 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00509 |
| Chain | Residue | Details |
| A | GLY39 | |
| B | GLY39 | |
| C | GLY39 | |
| D | GLY39 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1GCK |
| Chain | Residue | Details |
| A | TRP125 | |
| D | TRP125 | |
| D | ASN175 | |
| D | ARG361 | |
| A | ASN175 | |
| A | ARG361 | |
| B | TRP125 | |
| B | ASN175 | |
| B | ARG361 | |
| C | TRP125 | |
| C | ASN175 | |
| C | ARG361 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 |
| Chain | Residue | Details |
| A | LYS12 | |
| B | LYS12 | |
| C | LYS12 | |
| D | LYS12 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10029535, ECO:0000269|PubMed:11432784, ECO:0007744|PDB:1B5O, ECO:0007744|PDB:1B5P, ECO:0007744|PDB:5BJ3, ECO:0007744|PDB:5BJ4 |
| Chain | Residue | Details |
| A | LYS234 | |
| B | LYS234 | |
| C | LYS234 | |
| D | LYS234 |
