1YIY
Aedes aegypti kynurenine aminotransferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| A | 0097053 | biological_process | L-kynurenine catabolic process |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| B | 0097053 | biological_process | L-kynurenine catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR B 601 |
| Chain | Residue |
| B | GLU230 |
| B | SER318 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR A 602 |
| Chain | Residue |
| A | GLU230 |
| A | SER318 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR A 603 |
| Chain | Residue |
| A | TYR54 |
| A | HOH843 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR B 604 |
| Chain | Residue |
| B | GLU245 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BR A 605 |
| Chain | Residue |
| A | HIS234 |
| A | HOH755 |
| A | VAL228 |
| A | GLU233 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PMP A 500 |
| Chain | Residue |
| A | GLY109 |
| A | ALA110 |
| A | TYR111 |
| A | PHE135 |
| A | ASN189 |
| A | ASN193 |
| A | ASP221 |
| A | VAL223 |
| A | TYR224 |
| A | SER252 |
| A | LYS255 |
| A | LYS263 |
| A | HOH613 |
| A | HOH672 |
| B | TYR73 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PMP B 501 |
| Chain | Residue |
| A | TYR73 |
| A | HOH691 |
| B | GLY109 |
| B | ALA110 |
| B | TYR111 |
| B | PHE135 |
| B | ASN189 |
| B | ASN193 |
| B | ASP221 |
| B | TYR224 |
| B | SER252 |
| B | LYS255 |
| B | HOH610 |
| B | HOH640 |
| B | HOH665 |
| B | HOH690 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15853804, ECO:0000269|PubMed:18186649, ECO:0000312|PDB:1YIY, ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E |
| Chain | Residue | Details |
| A | TYR73 | |
| B | TYR73 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:15853804, ECO:0000269|PubMed:18186649, ECO:0000312|PDB:1YIY, ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E |
| Chain | Residue | Details |
| B | SER252 | |
| B | LYS263 | |
| A | ALA110 | |
| A | ASN193 | |
| A | TYR224 | |
| A | SER252 | |
| A | LYS263 | |
| B | ALA110 | |
| B | ASN193 | |
| B | TYR224 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18186649, ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E |
| Chain | Residue | Details |
| A | ARG405 | |
| B | ARG405 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:15853804, ECO:0000312|PDB:1YIY |
| Chain | Residue | Details |
| A | LYS255 | |
| B | LYS255 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
| Chain | Residue | Details |
| A | ASN6 | |
| A | ASN157 | |
| B | ASN6 | |
| B | ASN157 |
