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3HT5

Crystal Structure of IlvE a Branched Chain Amino Acid Transaminase from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004084molecular_functionbranched-chain-amino-acid transaminase activity
A0005515molecular_functionprotein binding
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_processL-valine biosynthetic process
A0016740molecular_functiontransferase activity
A0018272biological_processprotein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine
A0030170molecular_functionpyridoxal phosphate binding
A0052654molecular_functionL-leucine-2-oxoglutarate transaminase activity
A0052655molecular_functionL-valine-2-oxoglutarate transaminase activity
A0052656molecular_functionL-isoleucine-2-oxoglutarate transaminase activity
A0071267biological_processL-methionine salvage
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE PMP A 6236
ChainResidue
AARG101
ALEU268
AGLY270
AILE271
ATHR272
AGLY313
ATHR314
AHOH388
AHOH423
AHOH448
AHOH507
AARG194
ALYS204
ATYR209
AGLU240
AGLY242
AGLY243
AMET244
AASN245

Functional Information from PROSITE/UniProt
site_idPS00770
Number of Residues34
DetailsAA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EmGgmNIFfvlgsggsar..LvTpelsgsl.LpGItR
ChainResidueDetails
AGLU240-ARG273

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AARG101
ATYR209
AILE271
ATHR314

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS204

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1iyd
ChainResidueDetails
ALYS204

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PDB entries from 2025-06-18

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