1B5O
THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE MUTANT 1
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 | 6 |
Details | BINDING SITE FOR RESIDUE PO4 A 414 |
Chain | Residue |
A | GLY39 |
A | TRP125 |
A | ASN175 |
A | TYR322 |
A | ARG361 |
A | HOH579 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 414 |
Chain | Residue |
B | ARG361 |
B | HOH1596 |
B | TRP125 |
B | ASN175 |
B | TYR322 |
site_id | AC3 |
Number of Residues | 15 |
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 | LYS234 |
A | ARG242 |
A | HOH517 |
B | TYR64 |
B | HOH1564 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PLP B 413 |
Chain | Residue |
A | TYR64 |
A | HOH542 |
B | GLY99 |
B | GLY100 |
B | SER101 |
B | TRP125 |
B | ASN171 |
B | ASN175 |
B | ASP203 |
B | ILE205 |
B | TYR206 |
B | ALA233 |
B | LYS234 |
B | ARG242 |
B | HOH1521 |
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 | TRP125 | |
B | ASP203 |
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 | LYS234 | |
B | ASP203 | |
B | TYR128 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
B | ALA68 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
B | TYR124 | |
B | ASP203 |
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 | LYS234 | |
B | TRP125 | |
B | ASP203 |
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 | LYS234 | |
B | TYR124 | |
B | ASP203 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | TRP125 | |
A | ASP203 |