Structure of PDB 6le4 Chain A

Receptor sequence
>6le4A (length=380) Species: 1590 (Lactiplantibacillus plantarum) [Search protein sequence]
MKFETQLIHGGISEDATTGATSVPIYMASTFRQTKIGQNQYEYSRTGNPT
RAAVEALIATLEHGSAGFAFASGSAAINTVFSLFSAGDHIIVGNDVYGGT
FRLIDAVLKHFGMTFTAVDTRDLAAVEAAITPTTKAIYLETPTNPLLHIT
DIAAIAKLAQAHDLLSIIDNTFASPYVQKPLDLGVDIVLHSASAYLGGHS
DVIGGLVVTKTPALGEKIGYLQNAIGSILAPQESWLLQRGMKTLALRMQA
HLNNAAKIFTYLKSHPAVTKIYYPGDPDNPDFSIAKQQMNGFGAMISFEL
QPGMNPQTFVEHLQVITLAESLGALESLIEIPALMTHGAIPRTIRLQNGI
KDELIRLSVGVEASDDLLADLERGFASIQA
3D structure
PDB6le4 Catalytic specificity of the Lactobacillus plantarum cystathionine gamma-lyase presumed by the crystallographic analysis.
ChainA
Resolution3.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.4.1.1: cystathionine gamma-lyase.
4.4.1.8: Transferred entry: 4.4.1.13.
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 E9U A S72 G73 S74 Y97 R102 N144 D169 S191 E320 S321 L322 T336 R356 S72 G73 S74 Y97 R102 N144 D169 S191 E320 S321 L322 T336 R356
BS02 E9U A E42 Y43 R45 T46 N223 E42 Y43 R45 T46 N223
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003962 cystathionine gamma-synthase activity
GO:0004123 cystathionine gamma-lyase activity
GO:0016829 lyase activity
GO:0016846 carbon-sulfur lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0044540 L-cystine L-cysteine-lyase (deaminating)
GO:0080146 L-cysteine desulfhydrase activity
Biological Process
GO:0019346 transsulfuration
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6le4, PDBe:6le4, PDBj:6le4
PDBsum6le4
PubMed32913258
UniProtF9UT53

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