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5CM0

Crystal structure of branched-chain aminotransferase from thermophilic archaea Geoglobus acetivorans

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004084molecular_functionbranched-chain-amino-acid transaminase activity
A0005829cellular_componentcytosol
A0006532biological_processaspartate biosynthetic process
A0008483molecular_functiontransaminase activity
A0008652biological_processamino acid biosynthetic process
A0009081biological_processbranched-chain amino acid metabolic process
A0009082biological_processbranched-chain amino acid biosynthetic process
A0009097biological_processisoleucine biosynthetic process
A0009098biological_processL-leucine biosynthetic process
A0009099biological_processvaline biosynthetic process
A0046394biological_processcarboxylic acid biosynthetic process
A0050048molecular_functionL-leucine:2-oxoglutarate aminotransferase activity
A0052654molecular_functionL-leucine transaminase activity
A0052655molecular_functionL-valine transaminase activity
A0052656molecular_functionL-isoleucine transaminase activity
B0003824molecular_functioncatalytic activity
B0004084molecular_functionbranched-chain-amino-acid transaminase activity
B0005829cellular_componentcytosol
B0006532biological_processaspartate biosynthetic process
B0008483molecular_functiontransaminase activity
B0008652biological_processamino acid biosynthetic process
B0009081biological_processbranched-chain amino acid metabolic process
B0009082biological_processbranched-chain amino acid biosynthetic process
B0009097biological_processisoleucine biosynthetic process
B0009098biological_processL-leucine biosynthetic process
B0009099biological_processvaline biosynthetic process
B0046394biological_processcarboxylic acid biosynthetic process
B0050048molecular_functionL-leucine:2-oxoglutarate aminotransferase activity
B0052654molecular_functionL-leucine transaminase activity
B0052655molecular_functionL-valine transaminase activity
B0052656molecular_functionL-isoleucine transaminase activity
C0003824molecular_functioncatalytic activity
C0004084molecular_functionbranched-chain-amino-acid transaminase activity
C0005829cellular_componentcytosol
C0006532biological_processaspartate biosynthetic process
C0008483molecular_functiontransaminase activity
C0008652biological_processamino acid biosynthetic process
C0009081biological_processbranched-chain amino acid metabolic process
C0009082biological_processbranched-chain amino acid biosynthetic process
C0009097biological_processisoleucine biosynthetic process
C0009098biological_processL-leucine biosynthetic process
C0009099biological_processvaline biosynthetic process
C0046394biological_processcarboxylic acid biosynthetic process
C0050048molecular_functionL-leucine:2-oxoglutarate aminotransferase activity
C0052654molecular_functionL-leucine transaminase activity
C0052655molecular_functionL-valine transaminase activity
C0052656molecular_functionL-isoleucine transaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue PLP A 301
ChainResidue
AHIS50
AASP189
AASN190
ALEU208
AILE211
ATHR212
AGLY247
ATHR248
AHOH430
AHOH473
AARG53
AARG141
ALYS152
ATYR156
AASN159
AGLU185
ASER187
AGLY188

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL A 302
ChainResidue
AGLU129
ALYS130
APRO268

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL C 302
ChainResidue
CLYS130
CHOH412
CHOH546

site_idAC4
Number of Residues20
Detailsbinding site for residue PLP B 301
ChainResidue
BVAL33
BPHE34
BARG53
BCYS57
BARG141
BASN150
BILE151
BSER153
BTYR156
BASN159
BGLU185
BGLY188
BASP189
BGLY210
BILE211
BTHR212
BGLY247
BTHR248
BHOH428
BHOH463

site_idAC5
Number of Residues20
Detailsbinding site for residue PLP C 301
ChainResidue
CVAL33
CPHE34
CARG53
CCYS57
CARG141
CASN150
CILE151
CSER153
CTYR156
CASN159
CGLU185
CSER187
CGLY188
CGLY210
CILE211
CTHR212
CGLY247
CTHR248
CHOH426
CHOH444

Functional Information from PROSITE/UniProt
site_idPS00770
Number of Residues29
DetailsAA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EgSgdNIFivkngt......ItTpptlnn..LkGItR
ChainResidueDetails
AGLU185-ARG213

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PDB entries from 2024-06-12

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