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2COI

Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with gabapentin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0003824molecular_functioncatalytic activity
A0004084molecular_functionbranched-chain-amino-acid transaminase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0008483molecular_functiontransaminase activity
A0008652biological_processamino acid biosynthetic process
A0009081biological_processbranched-chain amino acid metabolic process
A0009082biological_processbranched-chain amino acid biosynthetic process
A0009098biological_processL-leucine biosynthetic process
A0009099biological_processvaline biosynthetic process
A0050048molecular_functionL-leucine:2-oxoglutarate aminotransferase activity
A0052654molecular_functionL-leucine transaminase activity
A0052655molecular_functionL-valine transaminase activity
A0052656molecular_functionL-isoleucine transaminase activity
B0000082biological_processG1/S transition of mitotic cell cycle
B0003824molecular_functioncatalytic activity
B0004084molecular_functionbranched-chain-amino-acid transaminase activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0008483molecular_functiontransaminase activity
B0008652biological_processamino acid biosynthetic process
B0009081biological_processbranched-chain amino acid metabolic process
B0009082biological_processbranched-chain amino acid biosynthetic process
B0009098biological_processL-leucine biosynthetic process
B0009099biological_processvaline biosynthetic process
B0050048molecular_functionL-leucine:2-oxoglutarate aminotransferase activity
B0052654molecular_functionL-leucine transaminase activity
B0052655molecular_functionL-valine transaminase activity
B0052656molecular_functionL-isoleucine transaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1430
ChainResidue
BASP133
BHOH1477
BHOH1745
BHOH1746
BHOH1747
BHOH1748

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP A 410
ChainResidue
ATYR227
AGLU257
ATHR260
ALEU286
AGLY288
AVAL289
ATHR290
ATHR333
AHOH430
AHOH461
AHOH575
AARG119
AARG212
ALYS222

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP B 410
ChainResidue
BARG119
BARG212
BLYS222
BTYR227
BGLU257
BTHR260
BASN262
BLEU286
BGLY288
BVAL289
BTHR290
BGLY332
BTHR333
BHOH1442
BHOH1445
BHOH1449

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GBN A 420
ChainResidue
ATYR161
AARG163
ATYR193
ATHR260
AGLY332
ATHR333
AALA334
AHOH508
AHOH555
AHOH560
BTYR90
BVAL175

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GBN B 420
ChainResidue
ATYR90
AVAL175
BTYR161
BARG163
BTYR193
BTHR260
BMET261
BGLY332
BTHR333
BALA334
BHOH1455

Functional Information from PROSITE/UniProt
site_idPS00770
Number of Residues35
DetailsAA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EvGtmNLFlywinedgeee.LaTppldgii.LpGVtR
ChainResidueDetails
AGLU257-ARG291

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS222
BLYS222

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1iyd
ChainResidueDetails
ALYS222

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1iyd
ChainResidueDetails
BLYS222

222036

PDB entries from 2024-07-03

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