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2QLR

Crystal structure of human kynurenine aminotransferase II

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 Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 426
ChainResidue
BASN328
BASP331

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL D 426
ChainResidue
CSER404
DMET33
DILE34
DSER35

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 427
ChainResidue
CHIS318
CARG321
CHOH562
CASN57
CTRP310
CGLY314

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 426
ChainResidue
ATHR21
AILE25

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL D 427
ChainResidue
DGLY64
DGLU65
DGLU66
DMET67

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL C 428
ChainResidue
CPHE325
CGLN329
CSER404
CALA405
CSER406
CPRO407
DASN42

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL D 428
ChainResidue
DASP138
DASP162
DGLY165
DVAL197
DASN201
DTHR204
DASN206
DHOH567
DHOH572

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 427
ChainResidue
AASP162
AGLU163
AHIS348

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL C 429
ChainResidue
CSER391
DHOH449

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL D 429
ChainResidue
DTHR8
DSER11
DARG14
DLYS123
DGLU126
DMET127
DHIS287
DHOH480
DHOH556

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 430
ChainResidue
CASN44
CMET45
CPHE46
CLYS49
CHOH542
DGLU56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues112
DetailsTransit peptide: {"description":"Mitochondrion","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues108
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]}
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

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PDB entries from 2025-12-17

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