Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0008483 | molecular_function | transaminase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0097052 | biological_process | L-kynurenine metabolic process |
B | 0005737 | cellular_component | cytoplasm |
B | 0008483 | molecular_function | transaminase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0097052 | biological_process | L-kynurenine metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP A 510 |
Chain | Residue |
A | GLY86 |
A | LYS222 |
A | ARG230 |
A | KMT520 |
A | HOH545 |
B | TYR57 |
A | ALA87 |
A | THR88 |
A | PHE112 |
A | ASN159 |
A | ASN163 |
A | ASP191 |
A | TYR194 |
A | SER219 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP B 1510 |
Chain | Residue |
A | TYR57 |
B | GLY86 |
B | ALA87 |
B | THR88 |
B | PHE112 |
B | ASN159 |
B | ASN163 |
B | ASP191 |
B | VAL193 |
B | TYR194 |
B | SER219 |
B | LYS222 |
B | ARG230 |
B | KMT1520 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE KMT A 520 |
Chain | Residue |
A | PHE15 |
A | GLN32 |
A | GLY33 |
A | ASN163 |
A | LYS222 |
A | PHE309 |
A | ARG347 |
A | PLP510 |
B | TYR57 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE KMT B 1520 |
Chain | Residue |
A | PHE253 |
B | GLY33 |
B | PHE112 |
B | ASN163 |
B | LYS222 |
B | PHE309 |
B | ARG347 |
B | PLP1510 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | LYS222 | |
A | PHE112 | |
A | ASP191 | |
site_id | CSA10 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
B | LYS222 | |
B | ASP191 | |
B | TYR115 | |
site_id | CSA11 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | PHE120 | |
A | LYS222 | |
A | ASP191 | |
site_id | CSA12 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
B | PHE120 | |
B | LYS222 | |
B | ASP191 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
B | LYS222 | |
B | PHE112 | |
B | ASP191 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | PHE111 | |
A | LYS222 | |
A | ASP191 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
B | PHE111 | |
B | LYS222 | |
B | ASP191 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | PHE111 | |
A | ARG213 | |
A | ASP191 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
B | PHE111 | |
B | ARG213 | |
B | ASP191 | |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | PHE112 | |
A | ASP191 | |
B | ALA61 | |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | ALA61 | |
B | PHE112 | |
B | ASP191 | |
site_id | CSA9 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | LYS222 | |
A | ASP191 | |
A | TYR115 | |