Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2VGZ

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
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
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
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLP A 1263
ChainResidue
AGLY116
AARG270
AHOH2154
BTYR74
ASER117
AGLN118
ATYR142
AASN202
ATYR233
ASER260
ASER262
ALYS263

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLP B 1263
ChainResidue
ATYR74
BGLY116
BSER117
BGLN118
BTYR142
BASN202
BPRO232
BTYR233
BSER260
BSER262
BLYS263
BARG270

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IOD A 1426
ChainResidue
AGLN119
ALYS123
BGLN119
BLYS123

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AARG20
BARG399
ATYR74
ATYR142
AASN202
AARG399
BARG20
BTYR74
BTYR142
BASN202

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9WVM8
ChainResidueDetails
ALYS69
ALYS179
ALYS422
BLYS69
BLYS179
BLYS422

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WVM8
ChainResidueDetails
ALYS263
ALYS339
ALYS367
BLYS263
BLYS339
BLYS367

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

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon