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1IUG

The crystal structure of aspartate aminotransferase which belongs to subgroup IV from Thermus thermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0004760molecular_functionL-serine-pyruvate transaminase activity
A0008453molecular_functionalanine-glyoxylate transaminase activity
A0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
B0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
B0004760molecular_functionL-serine-pyruvate transaminase activity
B0008453molecular_functionalanine-glyoxylate transaminase activity
B0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 B 3693
ChainResidue
ALYS85
AARG89
ALLP185
BARG28
BTRP229
BTHR230
BHOH2035
BHOH2102
BHOH2112

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 3694
ChainResidue
AHIS27
AALA228
ATHR230
BPHE86
BARG89
BLLP185

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues21
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. VDAAasGSQKglmcppGlGfV
ChainResidueDetails
AVAL176-VAL196

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bjo
ChainResidueDetails
ATYR83
AASP159

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bjo
ChainResidueDetails
BTYR83
BASP159

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bjo
ChainResidueDetails
APHE86
AASP159

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bjo
ChainResidueDetails
BPHE86
BASP159

247536

PDB entries from 2026-01-14

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