3E2Z
Crystal structure of mouse kynurenine aminotransferase III in complex with kynurenine
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 | 8 |
| Details | BINDING SITE FOR RESIDUE KYN A 456 |
| Chain | Residue |
| A | TRP54 |
| A | GLY72 |
| A | TYR160 |
| A | ASN219 |
| A | LLP281 |
| A | ARG430 |
| B | TYR98 |
| B | TYR312 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PMP B 456 |
| Chain | Residue |
| B | GLY134 |
| B | ALA135 |
| B | TYR136 |
| B | TYR160 |
| B | TYR163 |
| B | ASN215 |
| B | ASN219 |
| B | ASP247 |
| B | TYR250 |
| B | SER278 |
| B | LYS281 |
| B | LYS289 |
| B | KYN457 |
| A | TYR98 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE KYN B 457 |
| Chain | Residue |
| A | TYR98 |
| A | TYR312 |
| B | TRP54 |
| B | GLY72 |
| B | TYR160 |
| B | ASN219 |
| B | ARG430 |
| B | PMP456 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 457 |
| Chain | Residue |
| A | SER207 |
| A | HIS240 |
| A | ASP241 |
| A | HOH460 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 458 |
| Chain | Residue |
| A | ILE118 |
| A | GLU251 |
| A | TRP252 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 458 |
| Chain | Residue |
| B | GLN231 |
| B | ASP235 |
| B | VAL238 |
| B | PRO267 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 459 |
| Chain | Residue |
| B | SER207 |
| B | HIS240 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q16773 |
| Chain | Residue | Details |
| B | GLY72 | |
| B | ASN219 | |
| B | ARG430 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
| Chain | Residue | Details |
| B | LYS117 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:Q16773 |
| Chain | Residue | Details |
| B | LYS281 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS281 | |
| B | TYR160 | |
| B | ASP247 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ARG100 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR160 | |
| A | ASP247 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR160 | |
| B | ASP247 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR136 | |
| B | LYS281 | |
| B | ASP247 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR136 | |
| A | ASP247 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS281 | |
| B | ASP247 | |
| B | TYR163 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP247 | |
| A | TYR163 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS281 | |
| B | TYR250 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ARG100 |
