6MFB
Crystal structure of 3-hydroxykynurenine transaminase from Aedes aegypti
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004760 | molecular_function | L-serine-pyruvate transaminase activity |
| A | 0005777 | cellular_component | peroxisome |
| A | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009436 | biological_process | glyoxylate catabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| A | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| A | 0097053 | biological_process | L-kynurenine catabolic process |
| B | 0004760 | molecular_function | L-serine-pyruvate transaminase activity |
| B | 0005777 | cellular_component | peroxisome |
| B | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009436 | biological_process | glyoxylate catabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| B | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| B | 0097053 | biological_process | L-kynurenine catabolic process |
| C | 0004760 | molecular_function | L-serine-pyruvate transaminase activity |
| C | 0005777 | cellular_component | peroxisome |
| C | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009436 | biological_process | glyoxylate catabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| C | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| C | 0097053 | biological_process | L-kynurenine catabolic process |
| D | 0004760 | molecular_function | L-serine-pyruvate transaminase activity |
| D | 0005777 | cellular_component | peroxisome |
| D | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009436 | biological_process | glyoxylate catabolic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| D | 0047315 | molecular_function | kynurenine-glyoxylate transaminase activity |
| D | 0097053 | biological_process | L-kynurenine catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue PLP A 401 |
| Chain | Residue |
| A | SER77 |
| A | LYS205 |
| B | TYR256 |
| B | HIS258 |
| B | THR259 |
| A | ALA78 |
| A | HIS79 |
| A | TRP104 |
| A | GLY152 |
| A | SER154 |
| A | ASP179 |
| A | VAL181 |
| A | GLN204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Region: {"description":"Binds to and confers specificity for 3-hydroxykynurenine; shared with dimeric partner","evidences":[{"source":"UniProtKB","id":"Q7PRG3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of 3-hydroxykynurenine transaminase from Aedes aegypti.","authors":["Maciel L.G.","Oliveira A.A.","Romao T.P.","Silva Filha M.H.N.L.","dos Anjos J.V.","Soares T.A.","Guido R.V.C."]}},{"source":"PDB","id":"6MFB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q7PRG3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of 3-hydroxykynurenine transaminase from Aedes aegypti.","authors":["Maciel L.G.","Oliveira A.A.","Romao T.P.","Silva Filha M.H.N.L.","dos Anjos J.V.","Soares T.A.","Guido R.V.C."]}},{"source":"PDB","id":"6MFB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PIRSR","id":"PIRSR000524-50","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of 3-hydroxykynurenine transaminase from Aedes aegypti.","authors":["Maciel L.G.","Oliveira A.A.","Romao T.P.","Silva Filha M.H.N.L.","dos Anjos J.V.","Soares T.A.","Guido R.V.C."]}},{"source":"PDB","id":"6MFB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
