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3JZ6

Crystal structure of Mycobacterium smegmatis Branched Chain Aminotransferase in complex with pyridoxal-5'-phosphate at 1.9 angstrom.

Replaces:  3DTH
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004084molecular_functionbranched-chain-amino-acid transaminase activity
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
A0018272biological_processprotein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine
A0030170molecular_functionpyridoxal phosphate binding
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
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
B0018272biological_processprotein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine
B0030170molecular_functionpyridoxal phosphate binding
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 Residues18
DetailsBINDING SITE FOR RESIDUE PLP A 369
ChainResidue
AARG101
AILE271
ATHR272
AGLY313
ATHR314
AGOL370
AHOH382
AHOH387
AHOH396
AHOH450
AARG194
ALYS204
ATYR209
AGLU240
AGLY243
AASN245
ALEU268
AGLY270

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLP B 369
ChainResidue
BARG101
BARG194
BLYS204
BTYR209
BGLU240
BGLY243
BASN245
BLEU268
BGLY270
BILE271
BTHR272
BGLY313
BTHR314
BGOL370
BHOH373
BHOH380
BHOH432

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 370
ChainResidue
AARG194
AASN208
ATYR209
ASER212
ATRP229
AGLY242
AGLY243
APLP369

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 370
ChainResidue
BARG194
BASN208
BSER212
BTRP229
BGLY242
BPLP369
BHOH382

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20445230
ChainResidueDetails
AARG101
ATYR209
ATHR314
BARG101
BTYR209
BTHR314

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AILE271
BILE271

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS204
BLYS204

site_idSWS_FT_FI4
Number of Residues4
DetailsCROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) => ECO:0000269|PubMed:20094657
ChainResidueDetails
ALYS299
BLYS299

219140

PDB entries from 2024-05-01

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