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1IVR

STRUCTURE OF ASPARTATE AMINOTRANSFERASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006103biological_process2-oxoglutarate metabolic process
A0006520biological_processamino acid metabolic process
A0006531biological_processaspartate metabolic process
A0006533biological_processL-aspartate catabolic process
A0006536biological_processglutamate metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0016212molecular_functionkynurenine-oxoglutarate transaminase activity
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE CBA A 402
ChainResidue
AILE15
AASP214
ATYR217
ASER247
AALA249
ALYS250
AARG258
AARG284
AARG378
AHOH460
AVAL35
AGLY36
ATYR67
ASER104
AGLY105
ATHR106
ATRP133
AASN186

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYAKnmGLyGERAG
ChainResidueDetails
ASER247-GLY260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATRP133
AASP214
ALYS250

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATRP133
AASP214

246704

PDB entries from 2025-12-24

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