1GC4
THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2 COMPLEXED WITH ASPARTATE
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 | 9 |
| Details | BINDING SITE FOR RESIDUE ASP A 414 |
| Chain | Residue |
| A | GLY39 |
| A | TRP125 |
| A | ASN175 |
| A | LYS234 |
| A | TYR322 |
| A | ARG361 |
| A | PLP413 |
| B | TYR564 |
| B | ARG761 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ASP B 914 |
| Chain | Residue |
| A | TYR64 |
| A | ARG261 |
| B | VAL516 |
| B | TRP625 |
| B | ASN675 |
| B | TYR706 |
| B | LYS734 |
| B | TYR822 |
| B | ARG861 |
| B | PLP913 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ASP C 1414 |
| Chain | Residue |
| C | TRP1125 |
| C | ASN1175 |
| C | LYS1234 |
| C | TYR1322 |
| C | ARG1361 |
| C | PLP1413 |
| D | TYR1564 |
| D | ARG1761 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ASP D 1914 |
| Chain | Residue |
| C | TYR1064 |
| C | ARG1261 |
| D | TRP1625 |
| D | ASN1675 |
| D | LYS1734 |
| D | TYR1822 |
| D | ARG1861 |
| D | PLP1913 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 413 |
| Chain | Residue |
| A | GLY99 |
| A | GLY100 |
| A | SER101 |
| A | TRP125 |
| A | ASN171 |
| A | ASN175 |
| A | ASP203 |
| A | ILE205 |
| A | TYR206 |
| A | ALA233 |
| A | ARG242 |
| A | ASP414 |
| B | TYR564 |
| B | THR765 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 913 |
| Chain | Residue |
| A | TYR64 |
| B | GLY599 |
| B | GLY600 |
| B | SER601 |
| B | TRP625 |
| B | ASN671 |
| B | ASN675 |
| B | ASP703 |
| B | TYR706 |
| B | ALA733 |
| B | LYS734 |
| B | ARG742 |
| B | ASP914 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP C 1413 |
| Chain | Residue |
| C | GLY1099 |
| C | GLY1100 |
| C | SER1101 |
| C | TRP1125 |
| C | ASN1171 |
| C | ASN1175 |
| C | ASP1203 |
| C | ILE1205 |
| C | TYR1206 |
| C | ALA1233 |
| C | LYS1234 |
| C | ARG1242 |
| C | ASP1414 |
| D | TYR1564 |
| D | THR1765 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP D 1913 |
| Chain | Residue |
| C | TYR1064 |
| D | GLY1599 |
| D | GLY1600 |
| D | SER1601 |
| D | TRP1625 |
| D | ASN1671 |
| D | ASN1675 |
| D | ASP1703 |
| D | ILE1705 |
| D | TYR1706 |
| D | ALA1733 |
| D | ARG1742 |
| D | ASP1914 |
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 | GLY539 | |
| C | GLY1039 | |
| D | GLY1539 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1GCK |
| Chain | Residue | Details |
| A | TRP125 | |
| D | TRP1625 | |
| D | ASN1675 | |
| D | ARG1861 | |
| A | ASN175 | |
| A | ARG361 | |
| B | TRP625 | |
| B | ASN675 | |
| B | ARG861 | |
| C | TRP1125 | |
| C | ASN1175 | |
| C | ARG1361 |
| 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 | LYS512 | |
| C | LYS1012 | |
| D | LYS1512 |
| 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 | LYS734 | |
| C | LYS1234 | |
| D | LYS1734 |
