Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PLP A 500 |
Chain | Residue |
A | GLY126 |
A | SER277 |
A | LYS278 |
A | ARG286 |
A | ALA127 |
A | THR128 |
A | TYR152 |
A | ASN209 |
A | ASP237 |
A | ILE239 |
A | TYR240 |
A | SER275 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE AVG A 501 |
Chain | Residue |
A | LEU53 |
A | ALA54 |
A | TYR152 |
A | ALA154 |
A | LYS278 |
A | ARG412 |
A | HOH503 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SLSKdmGLpGFRVG |
Chain | Residue | Details |
A | SER275-GLY288 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU55 | |
A | TYR92 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | LYS278 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | TYR152 | |
A | ASP237 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | LYS278 | |
A | TYR152 | |
A | ASP237 | |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | ASP91 | |