Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0008483 | molecular_function | transaminase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0008483 | molecular_function | transaminase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GLU A 414 |
Chain | Residue |
A | GLY34 |
A | PHE121 |
A | ASN171 |
A | TYR320 |
A | ARG362 |
A | PLP413 |
A | HOH1330 |
B | TYR559 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GLU A 914 |
Chain | Residue |
A | THR264 |
B | GLY534 |
B | PHE621 |
B | ASN671 |
B | TYR702 |
B | LYS733 |
B | TYR820 |
B | ARG862 |
B | PLP913 |
A | TYR59 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PLP A 413 |
Chain | Residue |
A | GLY95 |
A | ALA96 |
A | ASN97 |
A | PHE121 |
A | ASN167 |
A | ASN171 |
A | ASP199 |
A | TYR202 |
A | SER232 |
A | LYS233 |
A | ARG241 |
A | GLU414 |
A | HOH1080 |
A | HOH1289 |
B | TYR559 |
B | HOH1129 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PLP B 913 |
Chain | Residue |
A | TYR59 |
A | GLU914 |
A | HOH1084 |
B | GLY595 |
B | ALA596 |
B | ASN597 |
B | PHE621 |
B | ASN667 |
B | ASN671 |
B | ASP699 |
B | TYR702 |
B | SER732 |
B | LYS733 |
B | ARG741 |
B | HOH1126 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GFSKtfAMtGWRLG |
Chain | Residue | Details |
A | GLY230-GLY243 | |