3FVU
Crystal Structure of Human Kynurenine Aminotransferase I in Complex with Indole-3-acetic Acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009617 | biological_process | response to bacterium |
| 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 | 0047316 | molecular_function | glutamine-phenylpyruvate 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 | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009617 | biological_process | response to bacterium |
| 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 | 0047316 | molecular_function | glutamine-phenylpyruvate 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 | 10 |
| Details | BINDING SITE FOR RESIDUE IAC A 423 |
| Chain | Residue |
| A | TRP18 |
| B | HIS279 |
| A | GLY36 |
| A | TYR101 |
| A | ASN185 |
| A | LLP247 |
| A | ARG398 |
| A | GOL425 |
| B | TYR63 |
| B | PHE278 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 424 |
| Chain | Residue |
| A | ALA77 |
| A | SER78 |
| A | GLU87 |
| A | ILE88 |
| A | HOH588 |
| A | HOH625 |
| B | LYS23 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 425 |
| Chain | Residue |
| A | GLN35 |
| A | GLY36 |
| A | IAC423 |
| A | HOH686 |
| B | HIS279 |
| B | HOH654 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 426 |
| Chain | Residue |
| A | PRO43 |
| A | ASP44 |
| A | PHE45 |
| A | HOH699 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 427 |
| Chain | Residue |
| A | HIS206 |
| A | HOH431 |
| A | HOH438 |
| A | HOH537 |
| A | HOH641 |
| A | HOH702 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE IAC B 423 |
| Chain | Residue |
| A | TYR63 |
| A | PHE278 |
| A | HIS279 |
| B | TRP18 |
| B | GLY36 |
| B | TYR101 |
| B | PHE125 |
| B | ASN185 |
| B | PHE339 |
| B | ARG398 |
| B | GOL424 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 424 |
| Chain | Residue |
| A | HIS279 |
| B | VAL22 |
| B | GLY36 |
| B | IAC423 |
| B | HOH526 |
| B | HOH628 |
| B | HOH700 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 425 |
| Chain | Residue |
| B | MET59 |
| B | LEU60 |
| B | GLN62 |
| B | TYR63 |
| B | THR64 |
| B | TYR69 |
| B | HOH662 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 426 |
| Chain | Residue |
| B | HIS206 |
| B | HOH447 |
| B | HOH529 |
| B | HOH530 |
| B | HOH658 |
| B | HOH703 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15364907, ECO:0007744|PDB:1W7M |
| Chain | Residue | Details |
| A | GLY36 | |
| A | ASN185 | |
| A | ARG398 | |
| B | GLY36 | |
| B | ASN185 | |
| B | ARG398 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:15364907, ECO:0007744|PDB:1W7L, ECO:0007744|PDB:1W7M |
| Chain | Residue | Details |
| A | LLP247 | |
| B | LLP247 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP213 | |
| A | PHE125 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP213 | |
| B | PHE125 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | PHE124 | |
| A | ASP213 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | PHE124 | |
| B | ASP213 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP213 | |
| A | TYR128 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP213 | |
| B | TYR128 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | GLU82 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | GLU82 |
