Structure of PDB 6e1j Chain B

Receptor sequence
>6e1jB (length=408) Species: 3707 (Brassica juncea) [Search protein sequence]
ERWPEYIPNKLPDKNYVRVFDTTLRDGEQSPGAALTPPQKIEIARQLAKL
RVDIMEVGFPVSSEEEFETIQTIAKTVGNEVDEETGYIPVICVIARSKER
DIKAAWESVKYAKRPRIVIFTSTSDIHLKYKLKMTREEVVDMVASSIRFA
KSLGFEDIEFGCEDGGRSDKDYICTVFEEAIKAGATTLACPDTVGINMPH
EYGKLVRYIKANTPGIDDVIFSAHCHNDLGVATANTIAGICAGARQVEVT
INGIGERSGNAPLEEVVMALKCRGAFVMGGVYTRIDTRQIMATSKMVQEY
TGLYVQPHKPIVGANCFVHESGIHQDGILKNRSTYEIISPEDVGVVKSQN
SGIVLGKLSGRHAVKGRLKELGYEISDEKLNEVFSRFRDLTKQKKRVTDD
DLKALVTC
3D structure
PDB6e1j Molecular Basis of the Evolution of Methylthioalkylmalate Synthase and the Diversity of Methionine-Derived Glucosinolates.
ChainB
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 COA B Q93 F123 S126 R160 F184 K195 Q29 F59 S62 R96 F120 K131
BS02 MN B D90 H288 H290 D26 H224 H226
BS03 KMT B R89 P255 T257 H288 H290 R25 P191 T193 H224 H226
BS04 COA B S385 G386 I387 D390 K394 L422 R425 H426 S321 G322 I323 D326 K330 L358 R361 H362
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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