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3FVX

Human kynurenine aminotransferase I in complex with tris

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0009617biological_processresponse to bacterium
A0016212molecular_functionkynurenine-oxoglutarate transaminase activity
A0016829molecular_functionlyase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042803molecular_functionprotein homodimerization activity
A0047316molecular_functionglutamine-phenylpyruvate transaminase activity
A0047804molecular_functioncysteine-S-conjugate beta-lyase activity
A0070189biological_processkynurenine metabolic process
A0097053biological_processL-kynurenine catabolic process
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0009617biological_processresponse to bacterium
B0016212molecular_functionkynurenine-oxoglutarate transaminase activity
B0016829molecular_functionlyase activity
B0030170molecular_functionpyridoxal phosphate binding
B0042803molecular_functionprotein homodimerization activity
B0047316molecular_functionglutamine-phenylpyruvate transaminase activity
B0047804molecular_functioncysteine-S-conjugate beta-lyase activity
B0070189biological_processkynurenine metabolic process
B0097053biological_processL-kynurenine catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS A 423
ChainResidue
AGLY36
AHOH760
BTYR63
APHE125
AASN185
ATYR216
ALLP247
APHE339
AARG398
AHOH456
AHOH661

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 424
ChainResidue
AHIS206
AHOH449
AHOH469
AHOH471
AHOH600
AHOH616

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 423
ChainResidue
BHIS206
BHOH464
BHOH562
BHOH609
BHOH707
BHOH716

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15364907, ECO:0007744|PDB:1W7M
ChainResidueDetails
AGLY36
AASN185
AARG398
BGLY36
BASN185
BARG398

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:15364907, ECO:0007744|PDB:1W7L, ECO:0007744|PDB:1W7M
ChainResidueDetails
ALLP247
BLLP247

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP213
APHE125

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP213
BPHE125

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
APHE124
AASP213

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BPHE124
BASP213

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP213
ATYR128

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP213
BTYR128

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AGLU82

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BGLU82

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PDB entries from 2024-07-24

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