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1AJS

REFINEMENT AND COMPARISON OF THE CRYSTAL STRUCTURES OF PIG CYTOSOLIC ASPARTATE AMINOTRANSFERASE AND ITS COMPLEX WITH 2-METHYLASPARTATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0004609molecular_functionphosphatidylserine decarboxylase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006103biological_process2-oxoglutarate metabolic process
A0006107biological_processoxaloacetate metabolic process
A0006114biological_processglycerol biosynthetic process
A0006520biological_processamino acid metabolic process
A0006531biological_processaspartate metabolic process
A0006532biological_processaspartate biosynthetic process
A0006533biological_processaspartate catabolic process
A0006536biological_processglutamate metabolic process
A0007219biological_processNotch signaling pathway
A0008483molecular_functiontransaminase activity
A0008652biological_processamino acid biosynthetic process
A0009058biological_processbiosynthetic process
A0019550biological_processglutamate catabolic process to aspartate
A0019551biological_processglutamate catabolic process to 2-oxoglutarate
A0030170molecular_functionpyridoxal phosphate binding
A0032869biological_processcellular response to insulin stimulus
A0047801molecular_functionL-cysteine transaminase activity
A0051384biological_processresponse to glucocorticoid
A0055089biological_processfatty acid homeostasis
B0003824molecular_functioncatalytic activity
B0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
B0004609molecular_functionphosphatidylserine decarboxylase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006103biological_process2-oxoglutarate metabolic process
B0006107biological_processoxaloacetate metabolic process
B0006114biological_processglycerol biosynthetic process
B0006520biological_processamino acid metabolic process
B0006531biological_processaspartate metabolic process
B0006532biological_processaspartate biosynthetic process
B0006533biological_processaspartate catabolic process
B0006536biological_processglutamate metabolic process
B0007219biological_processNotch signaling pathway
B0008483molecular_functiontransaminase activity
B0008652biological_processamino acid biosynthetic process
B0009058biological_processbiosynthetic process
B0019550biological_processglutamate catabolic process to aspartate
B0019551biological_processglutamate catabolic process to 2-oxoglutarate
B0030170molecular_functionpyridoxal phosphate binding
B0032869biological_processcellular response to insulin stimulus
B0047801molecular_functionL-cysteine transaminase activity
B0051384biological_processresponse to glucocorticoid
B0055089biological_processfatty acid homeostasis
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PLA A 415
ChainResidue
AASP222
ATYR225
ASER255
ASER257
ALYS258
AARG266
AARG386
AHOH562
BTYR70
BARG292
BHOH554
AVAL37
AGLY38
AGLY107
AGLY108
ATHR109
ATRP140
AASN194

site_idACT
Number of Residues1
DetailsCOENZYME BINDING SITES.
ChainResidue
BLLP258

site_idAXT
Number of Residues1
DetailsSUBSTRATE BINDING SITES.
ChainResidue
APLA415

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKnfGLyNERVG
ChainResidueDetails
ASER255-GLY268
BSER255-GLY268

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BALA39
BGLU141
BPRO195
BILE387

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
BASN259

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATRP140
AASP222
ALYS258

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTRP140
BASP222

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATRP140
AASP222

219140

PDB entries from 2024-05-01

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