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6MFB

Crystal structure of 3-hydroxykynurenine transaminase from Aedes aegypti

Functional Information from GO Data
ChainGOidnamespacecontents
A0004760molecular_functionL-serine-pyruvate transaminase activity
A0005777cellular_componentperoxisome
A0008453molecular_functionalanine-glyoxylate transaminase activity
A0008483molecular_functiontransaminase activity
A0009436biological_processglyoxylate catabolic process
A0016740molecular_functiontransferase activity
A0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
A0047315molecular_functionkynurenine-glyoxylate transaminase activity
A0097053biological_processL-kynurenine catabolic process
B0004760molecular_functionL-serine-pyruvate transaminase activity
B0005777cellular_componentperoxisome
B0008453molecular_functionalanine-glyoxylate transaminase activity
B0008483molecular_functiontransaminase activity
B0009436biological_processglyoxylate catabolic process
B0016740molecular_functiontransferase activity
B0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
B0047315molecular_functionkynurenine-glyoxylate transaminase activity
B0097053biological_processL-kynurenine catabolic process
C0004760molecular_functionL-serine-pyruvate transaminase activity
C0005777cellular_componentperoxisome
C0008453molecular_functionalanine-glyoxylate transaminase activity
C0008483molecular_functiontransaminase activity
C0009436biological_processglyoxylate catabolic process
C0016740molecular_functiontransferase activity
C0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
C0047315molecular_functionkynurenine-glyoxylate transaminase activity
C0097053biological_processL-kynurenine catabolic process
D0004760molecular_functionL-serine-pyruvate transaminase activity
D0005777cellular_componentperoxisome
D0008453molecular_functionalanine-glyoxylate transaminase activity
D0008483molecular_functiontransaminase activity
D0009436biological_processglyoxylate catabolic process
D0016740molecular_functiontransferase activity
D0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
D0047315molecular_functionkynurenine-glyoxylate transaminase activity
D0097053biological_processL-kynurenine catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue PLP A 401
ChainResidue
ASER77
ALYS205
BTYR256
BHIS258
BTHR259
AALA78
AHIS79
ATRP104
AGLY152
ASER154
AASP179
AVAL181
AGLN204

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsRegion: {"description":"Binds to and confers specificity for 3-hydroxykynurenine; shared with dimeric partner","evidences":[{"source":"UniProtKB","id":"Q7PRG3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q7PRG3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified 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"}]}
ChainResidueDetails

239149

数据于2025-07-23公开中

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