2R2N
The crystal structure of human kynurenine aminotransferase II in complex with kynurenine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006536 | biological_process | glutamate metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0033512 | biological_process | L-lysine catabolic process to acetyl-CoA via saccharopine |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| A | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
| A | 0047958 | molecular_function | glycine:2-oxoglutarate aminotransferase activity |
| A | 0050094 | molecular_function | methionine-glyoxylate transaminase activity |
| A | 0070189 | biological_process | kynurenine metabolic process |
| A | 1901605 | biological_process | alpha-amino acid metabolic process |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| B | 0006536 | biological_process | glutamate metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0033512 | biological_process | L-lysine catabolic process to acetyl-CoA via saccharopine |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| B | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
| B | 0047958 | molecular_function | glycine:2-oxoglutarate aminotransferase activity |
| B | 0050094 | molecular_function | methionine-glyoxylate transaminase activity |
| B | 0070189 | biological_process | kynurenine metabolic process |
| B | 1901605 | biological_process | alpha-amino acid metabolic process |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| C | 0006536 | biological_process | glutamate metabolic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0033512 | biological_process | L-lysine catabolic process to acetyl-CoA via saccharopine |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| C | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
| C | 0047958 | molecular_function | glycine:2-oxoglutarate aminotransferase activity |
| C | 0050094 | molecular_function | methionine-glyoxylate transaminase activity |
| C | 0070189 | biological_process | kynurenine metabolic process |
| C | 1901605 | biological_process | alpha-amino acid metabolic process |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| D | 0006536 | biological_process | glutamate metabolic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0033512 | biological_process | L-lysine catabolic process to acetyl-CoA via saccharopine |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| D | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
| D | 0047958 | molecular_function | glycine:2-oxoglutarate aminotransferase activity |
| D | 0050094 | molecular_function | methionine-glyoxylate transaminase activity |
| D | 0070189 | biological_process | kynurenine metabolic process |
| D | 1901605 | biological_process | alpha-amino acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PMP A 426 |
| Chain | Residue |
| A | SER117 |
| A | LYS263 |
| A | ARG270 |
| A | HOH572 |
| A | HOH661 |
| B | TYR74 |
| A | GLN118 |
| A | TYR142 |
| A | ASN202 |
| A | ASP230 |
| A | PRO232 |
| A | TYR233 |
| A | SER260 |
| A | SER262 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PMP B 426 |
| Chain | Residue |
| A | TYR74 |
| B | SER117 |
| B | GLN118 |
| B | TYR142 |
| B | ASN202 |
| B | ASP230 |
| B | PRO232 |
| B | TYR233 |
| B | SER260 |
| B | SER262 |
| B | LYS263 |
| B | ARG270 |
| B | HOH635 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PMP C 426 |
| Chain | Residue |
| C | SER117 |
| C | GLN118 |
| C | TYR142 |
| C | ASN202 |
| C | ASP230 |
| C | PRO232 |
| C | TYR233 |
| C | SER260 |
| C | SER262 |
| C | LYS263 |
| C | ARG270 |
| C | HOH694 |
| D | TYR74 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PMP D 426 |
| Chain | Residue |
| C | TYR74 |
| D | GLY116 |
| D | SER117 |
| D | GLN118 |
| D | TYR142 |
| D | ASN202 |
| D | ASP230 |
| D | PRO232 |
| D | TYR233 |
| D | SER260 |
| D | SER262 |
| D | LYS263 |
| D | ARG270 |
| D | HOH667 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE KYN A 427 |
| Chain | Residue |
| A | ILE19 |
| A | ARG20 |
| A | LEU293 |
| A | HOH515 |
| B | SER143 |
| B | ASN202 |
| B | ARG399 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE KYN C 427 |
| Chain | Residue |
| C | ILE19 |
| C | ARG20 |
| C | GLY39 |
| C | LEU40 |
| C | TYR74 |
| C | HOH635 |
| D | ASN202 |
| D | ARG399 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE KYN A 428 |
| Chain | Residue |
| A | TYR142 |
| A | ASN202 |
| A | ARG399 |
| A | HOH661 |
| B | ILE19 |
| B | ARG20 |
| B | GLY39 |
| B | TYR74 |
| B | HOH453 |
| B | HOH731 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE KYN C 428 |
| Chain | Residue |
| C | ASN202 |
| C | ARG399 |
| C | HOH657 |
| C | HOH703 |
| D | ILE19 |
| D | GLY39 |
| D | LEU40 |
| D | HOH638 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 427 |
| Chain | Residue |
| D | PRO76 |
| D | SER77 |
| D | ALA78 |
| D | GLY79 |
| D | LEU84 |
| D | HOH697 |
| D | HOH726 |
| D | HOH762 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 429 |
| Chain | Residue |
| C | HOH629 |
| C | HOH702 |
| C | GLU56 |
| C | ASN57 |
| C | HIS318 |
| C | ARG321 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 428 |
| Chain | Residue |
| D | GLU346 |
| D | TRP347 |
| D | HIS348 |
| D | TRP357 |
| D | TYR397 |
| D | HOH535 |
| D | HOH651 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 429 |
| Chain | Residue |
| C | MET45 |
| C | PHE46 |
| C | PRO47 |
| D | GLU56 |
| D | ASN57 |
| D | HIS318 |
| D | ARG321 |
| D | HOH660 |
| D | HOH759 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 430 |
| Chain | Residue |
| D | SER207 |
| D | LEU208 |
| D | THR209 |
| D | HOH503 |
| D | HOH533 |
| D | HOH555 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 429 |
| Chain | Residue |
| A | PRO43 |
| A | ASN44 |
| A | PHE46 |
| A | PHE48 |
| A | LYS49 |
| A | GLU65 |
| A | MET68 |
| A | LYS69 |
| A | LEU72 |
| A | HOH478 |
| A | HOH532 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ARG20 | |
| B | ARG399 | |
| C | ARG20 | |
| C | TYR74 | |
| C | TYR142 | |
| C | ASN202 | |
| C | ARG399 | |
| D | ARG20 | |
| D | TYR74 | |
| D | TYR142 | |
| D | ASN202 | |
| A | TYR74 | |
| D | ARG399 | |
| A | TYR142 | |
| A | ASN202 | |
| A | ARG399 | |
| B | ARG20 | |
| B | TYR74 | |
| B | TYR142 | |
| B | ASN202 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9WVM8 |
| Chain | Residue | Details |
| A | LYS69 | |
| D | LYS69 | |
| D | LYS179 | |
| D | LYS422 | |
| A | LYS179 | |
| A | LYS422 | |
| B | LYS69 | |
| B | LYS179 | |
| B | LYS422 | |
| C | LYS69 | |
| C | LYS179 | |
| C | LYS422 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WVM8 |
| Chain | Residue | Details |
| A | LYS263 | |
| D | LYS263 | |
| D | LYS339 | |
| D | LYS367 | |
| A | LYS339 | |
| A | LYS367 | |
| B | LYS263 | |
| B | LYS339 | |
| B | LYS367 | |
| C | LYS263 | |
| C | LYS339 | |
| C | LYS367 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR142 | |
| A | LYS263 | |
| A | ASP230 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR142 | |
| B | LYS263 | |
| B | ASP230 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | TYR142 | |
| C | LYS263 | |
| C | ASP230 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | TYR142 | |
| D | LYS263 | |
| D | ASP230 |
