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1AMA

DOMAIN CLOSURE IN MITOCHONDRIAL 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_processaspartate catabolic process
A0006536biological_processglutamate metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0016212molecular_functionkynurenine-oxoglutarate transaminase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLA A 411
ChainResidue
AILE17
AVAL37
AGLY38
ATYR70
ASER107
AGLY108
ATHR109
ATRP140
AASN194
AASP222
ATYR225
ASER255
ALYS258
AARG266
AARG292
AARG386
AHOH468

site_idACT
Number of Residues24
DetailsACTIVE SITE WHICH COMPRISES THE COFACTOR BINDING SITE AND THE CATALYTIC SITE
ChainResidue
AASP15
ATHR109
ATRP140
AASN194
AASP222
AALA224
ATYR225
ASER255
ALYS258
AARG266
AARG292
AILE17
ASER296
AASN297
APHE360
AARG386
APLA411
ALEU18
AVAL37
AGLY38
AALA39
ATYR70
ASER107
AGLY108

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

223790

PDB entries from 2024-08-14

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