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6EZL

Crystal structure of aspartate aminotransferase from Trypanosoma cruzi at 2.07 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0006532biological_processaspartate biosynthetic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0003824molecular_functioncatalytic activity
B0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0006532biological_processaspartate biosynthetic process
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue PLP A 501
ChainResidue
AHIS44
ATYR215
ASER245
ASER247
ALYS248
AHOH643
BSER286
ASER101
AGLY102
ATHR103
ALEU106
ATRP130
AASN184
AASP212
AALA214

site_idAC2
Number of Residues20
Detailsbinding site for Di-peptide PLP B 501 and LYS B 248
ChainResidue
ASER286
BHIS44
BPRO45
BSER101
BGLY102
BTHR103
BTRP130
BASN184
BASP212
BALA214
BTYR215
BTYR218
BSER245
BTYR246
BSER247
BASN249
BMET250
BTYR253
BHOH663
BHOH669

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKnmGLyAERVG
ChainResidueDetails
ASER245-GLY258

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PDB entries from 2024-06-12

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