2R5C
Aedes Kynurenine Aminotransferase in Complex with Cysteine
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 | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| A | 0070189 | biological_process | kynurenine metabolic process |
| 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 | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0047315 | molecular_function | kynurenine-glyoxylate transaminase 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 | 19 |
| Details | BINDING SITE FOR RESIDUE C6P B 430 |
| Chain | Residue |
| A | TYR73 |
| B | ASN193 |
| B | ASP221 |
| B | TYR224 |
| B | SER252 |
| B | LYS255 |
| B | LYS263 |
| B | PHE347 |
| B | ARG405 |
| B | HOH698 |
| B | HOH708 |
| B | TRP27 |
| B | GLN44 |
| B | GLY45 |
| B | GLY109 |
| B | ALA110 |
| B | TYR111 |
| B | PHE135 |
| B | ASN189 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15853804","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18186649","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YIY","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2R5C","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2R5E","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"15853804","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18186649","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YIY","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2R5C","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2R5E","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18186649","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2R5C","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2R5E","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"15853804","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YIY","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| 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 | ASP221 | |
| A | PHE135 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ARG81 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP221 | |
| B | PHE135 | |
| B | LYS255 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP221 | |
| B | PHE135 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR111 | |
| A | ASP221 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR111 | |
| B | ASP221 | |
| B | LYS255 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP221 | |
| A | TYR138 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP221 | |
| B | TYR138 | |
| B | LYS255 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR224 | |
| B | LYS255 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ARG81 |
