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3B46

Crystal Structure of Bna3p, a Putative Kynurenine Aminotransferase from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0001558biological_processregulation of cell growth
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0016212molecular_functionkynurenine-oxoglutarate transaminase activity
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0034276biological_processkynurenic acid biosynthetic process
A0047536molecular_function2-aminoadipate transaminase activity
A0097053biological_processL-kynurenine catabolic process
B0001558biological_processregulation of cell growth
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0016212molecular_functionkynurenine-oxoglutarate transaminase activity
B0016740molecular_functiontransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0034276biological_processkynurenic acid biosynthetic process
B0047536molecular_function2-aminoadipate transaminase activity
B0097053biological_processL-kynurenine catabolic process
Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SAGKsfAAtGWRIG
ChainResidueDetails
ASER268-GLY281

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALLP271
BLLP271

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP237
APHE149

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP237
BPHE149

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR152
AASP237

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTYR152
BASP237

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR152
AARG251
AASP237

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTYR152
BARG251
BASP237

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
APRO107

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BPRO107

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PDB entries from 2024-07-31

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