1GCK
THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 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 | 0006520 | biological_process | amino acid 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 | 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 | 0006520 | biological_process | amino acid 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 | 0033853 | molecular_function | aspartate-prephenate aminotransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ASP A 414 |
| Chain | Residue |
| A | GLY39 |
| A | TRP125 |
| A | ASN175 |
| A | LYS234 |
| A | ARG361 |
| A | PLP413 |
| B | TYR564 |
| B | ARG761 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ASP B 914 |
| Chain | Residue |
| B | THR516 |
| B | GLY539 |
| B | TRP625 |
| B | ASN675 |
| B | LYS734 |
| B | TYR822 |
| B | ARG861 |
| B | PLP913 |
| A | ARG261 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 413 |
| Chain | Residue |
| A | GLY100 |
| A | SER101 |
| A | TRP125 |
| A | TYR128 |
| A | ASN171 |
| A | ASN175 |
| A | ASP203 |
| A | ILE205 |
| A | TYR206 |
| A | ALA233 |
| A | LYS234 |
| A | ARG242 |
| A | ASP414 |
| B | TYR564 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP B 913 |
| Chain | Residue |
| A | TYR64 |
| B | GLY599 |
| B | GLY600 |
| B | SER601 |
| B | TRP625 |
| B | ASN675 |
| B | ASP703 |
| B | ILE705 |
| B | TYR706 |
| B | LYS734 |
| B | ARG742 |
| B | ASP914 |
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 | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00509","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1GCK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for prephenate aminotransferase activity","evidences":[{"source":"PubMed","id":"30771275","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10029535","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11432784","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B5O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1B5P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5BJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5BJ4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR124 | |
| A | ASP203 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TRP625 | |
| B | ASP703 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS234 | |
| A | ASP203 | |
| A | TYR128 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS734 | |
| B | TYR628 | |
| B | ASP703 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ALA568 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR624 | |
| B | ASP703 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ALA68 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS234 | |
| A | TRP125 | |
| A | ASP203 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS734 | |
| B | TRP625 | |
| B | ASP703 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS234 | |
| A | TYR124 | |
| A | ASP203 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS734 | |
| B | TYR624 | |
| B | ASP703 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TRP125 | |
| A | ASP203 |
