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9AAT

X-RAY STRUCTURE REFINEMENT AND COMPARISON OF THREE FORMS OF MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0004838molecular_functionL-tyrosine:2-oxoglutarate aminotransferase activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006103biological_process2-oxoglutarate metabolic process
A0006520biological_processamino acid metabolic process
A0006531biological_processaspartate metabolic process
A0006533biological_processaspartate catabolic process
A0006536biological_processglutamate metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0016212molecular_functionkynurenine-oxoglutarate transaminase activity
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0033585biological_processL-phenylalanine biosynthetic process from chorismate via phenylpyruvate
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0097052biological_processL-kynurenine metabolic process
B0003824molecular_functioncatalytic activity
B0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
B0004838molecular_functionL-tyrosine:2-oxoglutarate aminotransferase activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0006103biological_process2-oxoglutarate metabolic process
B0006520biological_processamino acid metabolic process
B0006531biological_processaspartate metabolic process
B0006533biological_processaspartate catabolic process
B0006536biological_processglutamate metabolic process
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0016212molecular_functionkynurenine-oxoglutarate transaminase activity
B0016740molecular_functiontransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0033585biological_processL-phenylalanine biosynthetic process from chorismate via phenylpyruvate
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0097052biological_processL-kynurenine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PMP A 411
ChainResidue
ASER107
AGLY108
ATHR109
ALEU112
ATRP140
AASN194
AASP222
AALA224
ATYR225
ASER255
ALYS258
AARG266
BTYR70
BHOH642

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PMP B 411
ChainResidue
ATYR70
AHOH622
BSER107
BGLY108
BTHR109
BLEU112
BTRP140
BASN194
BASP222
BTYR225
BSER255
BALA257
BLYS258
BARG266
BHOH429

site_idACA
Number of Residues23
DetailsACTIVE SITE, COMPRISES THE COFACTOR BINDING SITE AND CATALYTIC SITE
ChainResidue
AASP15
ATHR109
ATRP140
AASN194
AASP222
AALA224
ATYR225
ASER255
ALYS258
AARG266
AARG292
AILE17
ASER296
AASN297
APHE360
AARG386
ALEU18
AVAL37
AGLY38
AALA39
ATYR70
ASER107
AGLY108

site_idACB
Number of Residues23
DetailsACTIVE SITE, COMPRISES THE COFACTOR BINDING SITE AND CATALYTIC SITE
ChainResidue
BASP15
BILE17
BLEU18
BVAL37
BGLY38
BALA39
BTYR70
BSER107
BGLY108
BTHR109
BTRP140
BASN194
BASP222
BALA224
BTYR225
BSER255
BLYS258
BARG266
BARG292
BSER296
BASN297
BPHE360
BARG386

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYAKnmGLyGERAG
ChainResidueDetails
ASER255-GLY268

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AGLY38
ATRP140
AASN194
AARG386
BGLY38
BTRP140
BASN194
BARG386

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS258
BLYS258

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PDB entries from 2024-04-24

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