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1OXP

ASPARTATE AMINOTRANSFERASE, H-ASP COMPLEX, CLOSED CONFORMATION

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 Residues16
DetailsBINDING SITE FOR RESIDUE IK2 A 411
ChainResidue
AILE17
ASER255
AALA257
ALYS258
AARG266
AARG292
AHOH461
AHOH625
ATYR70
ASER107
AGLY108
ATHR109
ATRP140
AASN194
AASP222
ATYR225

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 Residues4
DetailsBINDING:
ChainResidueDetails
AGLY38
ATRP140
AASN194
AARG386

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS258

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
ATRP140
AASP222

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PDB entries from 2025-06-18

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