3E2F
Crystal structure of mouse kynurenine aminotransferase III, PLP-bound form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| A | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| A | 0070189 | biological_process | kynurenine metabolic process |
| A | 0097053 | biological_process | L-kynurenine catabolic process |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| B | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| B | 0070189 | biological_process | kynurenine metabolic process |
| B | 0097053 | biological_process | L-kynurenine catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 456 |
| Chain | Residue |
| A | GLN71 |
| A | GLY72 |
| A | TYR160 |
| A | ASN219 |
| A | PHE373 |
| A | ARG430 |
| A | GOL457 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 457 |
| Chain | Residue |
| A | TYR160 |
| A | ASP161 |
| A | GOL456 |
| A | TRP54 |
| A | TYR136 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 458 |
| Chain | Residue |
| A | ARG180 |
| A | SER181 |
| A | THR195 |
| A | ASP197 |
| B | ARG180 |
| B | SER181 |
| B | LYS182 |
| B | THR195 |
| B | ASP197 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 459 |
| Chain | Residue |
| A | GLN231 |
| A | ASP235 |
| A | PRO267 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 460 |
| Chain | Residue |
| A | GLU152 |
| A | SER203 |
| A | LYS204 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 461 |
| Chain | Residue |
| A | ASP241 |
| A | GLU271 |
| A | ARG272 |
| A | HIS298 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 456 |
| Chain | Residue |
| A | TYR312 |
| B | ASN52 |
| B | TRP54 |
| B | TYR136 |
| B | ASP161 |
| B | GOL457 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 457 |
| Chain | Residue |
| B | TRP54 |
| B | GLN71 |
| B | GLY72 |
| B | ASN219 |
| B | TYR250 |
| B | PHE373 |
| B | ARG430 |
| B | GOL456 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 458 |
| Chain | Residue |
| B | ILE118 |
| B | GLU251 |
| B | TRP252 |
| B | HOH494 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 459 |
| Chain | Residue |
| B | GLN231 |
| B | ASP235 |
| B | VAL238 |
| B | PRO267 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q16773 |
| Chain | Residue | Details |
| A | GLY72 | |
| A | ASN219 | |
| A | ARG430 | |
| B | GLY72 | |
| B | ASN219 | |
| B | ARG430 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
| Chain | Residue | Details |
| A | LYS117 | |
| B | LYS117 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:Q16773 |
| Chain | Residue | Details |
| A | LLP281 | |
| B | LLP281 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR160 | |
| A | ASP247 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR160 | |
| B | ASP247 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR136 | |
| A | ASP247 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR136 | |
| B | ASP247 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP247 | |
| A | TYR163 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP247 | |
| B | TYR163 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ARG100 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ARG100 |
