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3DC1

Crystal structure of kynurenine aminotransferase II complex with alpha-ketoglutarate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006103biological_process2-oxoglutarate metabolic process
A0006536biological_processglutamate metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0016212molecular_functionkynurenine-oxoglutarate transaminase activity
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0033512biological_processL-lysine catabolic process to acetyl-CoA via saccharopine
A0042803molecular_functionprotein homodimerization activity
A0047315molecular_functionkynurenine-glyoxylate transaminase activity
A0047536molecular_function2-aminoadipate transaminase activity
A0047958molecular_functionglycine:2-oxoglutarate aminotransferase activity
A0050094molecular_functionmethionine-glyoxylate transaminase activity
A0070189biological_processkynurenine metabolic process
A1901605biological_processalpha-amino acid metabolic process
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006103biological_process2-oxoglutarate metabolic process
B0006536biological_processglutamate metabolic process
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0016212molecular_functionkynurenine-oxoglutarate transaminase activity
B0016740molecular_functiontransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0033512biological_processL-lysine catabolic process to acetyl-CoA via saccharopine
B0042803molecular_functionprotein homodimerization activity
B0047315molecular_functionkynurenine-glyoxylate transaminase activity
B0047536molecular_function2-aminoadipate transaminase activity
B0047958molecular_functionglycine:2-oxoglutarate aminotransferase activity
B0050094molecular_functionmethionine-glyoxylate transaminase activity
B0070189biological_processkynurenine metabolic process
B1901605biological_processalpha-amino acid metabolic process
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0006103biological_process2-oxoglutarate metabolic process
C0006536biological_processglutamate metabolic process
C0008483molecular_functiontransaminase activity
C0009058biological_processbiosynthetic process
C0016212molecular_functionkynurenine-oxoglutarate transaminase activity
C0016740molecular_functiontransferase activity
C0030170molecular_functionpyridoxal phosphate binding
C0033512biological_processL-lysine catabolic process to acetyl-CoA via saccharopine
C0042803molecular_functionprotein homodimerization activity
C0047315molecular_functionkynurenine-glyoxylate transaminase activity
C0047536molecular_function2-aminoadipate transaminase activity
C0047958molecular_functionglycine:2-oxoglutarate aminotransferase activity
C0050094molecular_functionmethionine-glyoxylate transaminase activity
C0070189biological_processkynurenine metabolic process
C1901605biological_processalpha-amino acid metabolic process
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0006103biological_process2-oxoglutarate metabolic process
D0006536biological_processglutamate metabolic process
D0008483molecular_functiontransaminase activity
D0009058biological_processbiosynthetic process
D0016212molecular_functionkynurenine-oxoglutarate transaminase activity
D0016740molecular_functiontransferase activity
D0030170molecular_functionpyridoxal phosphate binding
D0033512biological_processL-lysine catabolic process to acetyl-CoA via saccharopine
D0042803molecular_functionprotein homodimerization activity
D0047315molecular_functionkynurenine-glyoxylate transaminase activity
D0047536molecular_function2-aminoadipate transaminase activity
D0047958molecular_functionglycine:2-oxoglutarate aminotransferase activity
D0050094molecular_functionmethionine-glyoxylate transaminase activity
D0070189biological_processkynurenine metabolic process
D1901605biological_processalpha-amino acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE AKG A 426
ChainResidue
APRO18
AGLY39
ALEU293
BTYR142
BLLP263

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 427
ChainResidue
BTYR74
BLEU293
AGLN118
ATYR142
ALLP263
BILE19

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 428
ChainResidue
APRO16
APRO18
AHOH653

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 426
ChainResidue
CILE19
CGLY39
CTYR74
DGLN118
DLLP263

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL C 427
ChainResidue
CGLY29
CPRO30
DVAL375

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 426
ChainResidue
CTYR142
CTYR233
CLLP263
CMET354
DILE19
DGLY39
DTYR74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues108
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues19
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues28
DetailsTransit peptide: {"description":"Mitochondrion","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR142
AASP230

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTYR142
BASP230

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
CTYR142
CASP230

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
DTYR142
DASP230

239149

PDB entries from 2025-07-23

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