Structure of PDB 6le4 Chain D

Receptor sequence
>6le4D (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.
ChainD
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 D Y43 R45 T46 N223 Y43 R45 T46 N223
BS02 E9U D 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
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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