Structure of PDB 6e1j Chain A

Receptor sequence
>6e1jA (length=409) Species: 3707 (Brassica juncea) [Search protein sequence]
VERWPEYIPNKLPDKNYVRVFDTTLRDGEQSPGAALTPPQKIEIARQLAK
LRVDIMEVGFPVSSEEEFETIQTIAKTVGNEVDEETGYIPVICVIARSKE
RDIKAAWESVKYAKRPRIVIFTSTSDIHLKYKLKMTREEVVDMVASSIRF
AKSLGFEDIEFGCEDGGRSDKDYICTVFEEAIKAGATTLACPDTVGINMP
HEYGKLVRYIKANTPGIDDVIFSAHCHNDLGVATANTIAGICAGARQVEV
TINGIGERSGNAPLEEVVMALKCRGAFVMGGVYTRIDTRQIMATSKMVQE
YTGLYVQPHKPIVGANCFVHESGIHQDGILKNRSTYEIISPEDVGVVKSQ
NSGIVLGKLSGRHAVKGRLKELGYEISDEKLNEVFSRFRDLTKQKKRVTD
DDLKALVTC
3D structure
PDB6e1j Molecular Basis of the Evolution of Methylthioalkylmalate Synthase and the Diversity of Methionine-Derived Glucosinolates.
ChainA
Resolution2.096 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MN A D90 H288 H290 D27 H225 H227
BS02 MN A V145 E147 V82 E84
BS03 KMT A P255 T257 H288 H290 P192 T194 H225 H227
BS04 COA A S385 G386 I387 D390 K394 L422 R425 H426 S322 G323 I324 D327 K331 L359 R362 H363
BS05 COA A Q93 F123 S126 I158 R160 F184 K195 L196 Q30 F60 S63 I95 R97 F121 K132 L133
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003852 2-isopropylmalate synthase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer
Biological Process
GO:0009098 L-leucine biosynthetic process
GO:0019752 carboxylic acid metabolic process
GO:0043436 oxoacid metabolic process
Cellular Component
GO:0009507 chloroplast

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6e1j, PDBe:6e1j, PDBj:6e1j
PDBsum6e1j
PubMed31023839
UniProtC5J4P1

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