2QLR
Crystal structure of human kynurenine aminotransferase II
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009063 | biological_process | amino acid catabolic process |
| A | 0016212 | molecular_function | L-kynurenine:2-oxoglutarate transaminase activity |
| A | 0019477 | biological_process | L-lysine catabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0047313 | molecular_function | aromatic-amino-acid:glyoxylate transaminase activity |
| A | 0047315 | molecular_function | L-kynurenine:glyoxylate transaminase activity |
| A | 0047536 | molecular_function | L-2-aminoadipate:2-oxoglutarate transaminase activity |
| A | 0047958 | molecular_function | glycine:2-oxoglutarate transaminase activity |
| A | 0050094 | molecular_function | L-methionine:glyoxylate transaminase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009063 | biological_process | amino acid catabolic process |
| B | 0016212 | molecular_function | L-kynurenine:2-oxoglutarate transaminase activity |
| B | 0019477 | biological_process | L-lysine catabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0047313 | molecular_function | aromatic-amino-acid:glyoxylate transaminase activity |
| B | 0047315 | molecular_function | L-kynurenine:glyoxylate transaminase activity |
| B | 0047536 | molecular_function | L-2-aminoadipate:2-oxoglutarate transaminase activity |
| B | 0047958 | molecular_function | glycine:2-oxoglutarate transaminase activity |
| B | 0050094 | molecular_function | L-methionine:glyoxylate transaminase activity |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0005829 | cellular_component | cytosol |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0009063 | biological_process | amino acid catabolic process |
| C | 0016212 | molecular_function | L-kynurenine:2-oxoglutarate transaminase activity |
| C | 0019477 | biological_process | L-lysine catabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0047313 | molecular_function | aromatic-amino-acid:glyoxylate transaminase activity |
| C | 0047315 | molecular_function | L-kynurenine:glyoxylate transaminase activity |
| C | 0047536 | molecular_function | L-2-aminoadipate:2-oxoglutarate transaminase activity |
| C | 0047958 | molecular_function | glycine:2-oxoglutarate transaminase activity |
| C | 0050094 | molecular_function | L-methionine:glyoxylate transaminase activity |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0005829 | cellular_component | cytosol |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0009063 | biological_process | amino acid catabolic process |
| D | 0016212 | molecular_function | L-kynurenine:2-oxoglutarate transaminase activity |
| D | 0019477 | biological_process | L-lysine catabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0047313 | molecular_function | aromatic-amino-acid:glyoxylate transaminase activity |
| D | 0047315 | molecular_function | L-kynurenine:glyoxylate transaminase activity |
| D | 0047536 | molecular_function | L-2-aminoadipate:2-oxoglutarate transaminase activity |
| D | 0047958 | molecular_function | glycine:2-oxoglutarate transaminase activity |
| D | 0050094 | molecular_function | L-methionine:glyoxylate transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 426 |
| Chain | Residue |
| B | ASN328 |
| B | ASP331 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 426 |
| Chain | Residue |
| C | SER404 |
| D | MET33 |
| D | ILE34 |
| D | SER35 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 427 |
| Chain | Residue |
| C | HIS318 |
| C | ARG321 |
| C | HOH562 |
| C | ASN57 |
| C | TRP310 |
| C | GLY314 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 426 |
| Chain | Residue |
| A | THR21 |
| A | ILE25 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 427 |
| Chain | Residue |
| D | GLY64 |
| D | GLU65 |
| D | GLU66 |
| D | MET67 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 428 |
| Chain | Residue |
| C | PHE325 |
| C | GLN329 |
| C | SER404 |
| C | ALA405 |
| C | SER406 |
| C | PRO407 |
| D | ASN42 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 428 |
| Chain | Residue |
| D | ASP138 |
| D | ASP162 |
| D | GLY165 |
| D | VAL197 |
| D | ASN201 |
| D | THR204 |
| D | ASN206 |
| D | HOH567 |
| D | HOH572 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 427 |
| Chain | Residue |
| A | ASP162 |
| A | GLU163 |
| A | HIS348 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C 429 |
| Chain | Residue |
| C | SER391 |
| D | HOH449 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 429 |
| Chain | Residue |
| D | THR8 |
| D | SER11 |
| D | ARG14 |
| D | LYS123 |
| D | GLU126 |
| D | MET127 |
| D | HIS287 |
| D | HOH480 |
| D | HOH556 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 430 |
| Chain | Residue |
| C | ASN44 |
| C | MET45 |
| C | PHE46 |
| C | LYS49 |
| C | HOH542 |
| D | GLU56 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 112 |
| Details | Transit peptide: {"description":"Mitochondrion","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 108 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR142 | |
| A | ASP230 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR142 | |
| B | ASP230 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | TYR142 | |
| C | ASP230 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | TYR142 | |
| D | ASP230 |
