5VEH
Re-refinement OF THE PDB STRUCTURE 1yiz of 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 | 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 | 2 |
| Details | binding site for residue BR A 501 |
| Chain | Residue |
| A | GLU230 |
| A | MET322 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue BR A 502 |
| Chain | Residue |
| A | TYR54 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue BR A 503 |
| Chain | Residue |
| A | GLY242 |
| A | TRP244 |
| A | GLU245 |
| A | HOH901 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue BR A 504 |
| Chain | Residue |
| A | GOL508 |
| A | HOH862 |
| A | ARG201 |
| A | GLU205 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue BR A 505 |
| Chain | Residue |
| A | ASN41 |
| A | GLN384 |
| A | HOH916 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue BR A 506 |
| Chain | Residue |
| A | ARG201 |
| A | ALA202 |
| A | HOH964 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue BR A 507 |
| Chain | Residue |
| B | BR504 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 508 |
| Chain | Residue |
| A | TYR37 |
| A | LYS212 |
| A | PRO241 |
| A | THR378 |
| A | LYS379 |
| A | GLY382 |
| A | BR504 |
| A | HOH646 |
| A | HOH729 |
| A | HOH736 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue BR B 501 |
| Chain | Residue |
| B | GLU230 |
| B | MET322 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue BR B 502 |
| Chain | Residue |
| B | GLU245 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue BR B 503 |
| Chain | Residue |
| B | PRO140 |
| B | HOH699 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue BR B 504 |
| Chain | Residue |
| A | ILE31 |
| A | BR507 |
| B | GLY76 |
| B | TYR286 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue BR B 505 |
| Chain | Residue |
| B | GLN44 |
| B | GLN384 |
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 |
