Structure of PDB 5x5h Chain A Binding Site BS02
Receptor Information
>5x5h Chain A (length=385) Species:
196627
(Corynebacterium glutamicum ATCC 13032) [
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FDPNTQGFSTASIHAGYEPDDYYGSINTPIYASTTFAQNAPNELRKGYEY
TRVGNPTIVALEQTVAALEGAKYGRAFSSGMAATDILFRIILKPGDHIVL
GNDAYGGTYRLIDTVFTAWGVEYTVVDTSVVEEVKAAIKDNTKLIWVETP
TNPALGITDIEAVAKLTEGTNAKLVVDNTFASPYLQQPLKLGAHAVLHST
TKYIGGHSDVVGGLVVTNDQEMDEELLFMQGGIGPIPSVFDAYLTARGLK
TLAVRMDRHCDNAEKIAEFLDSRPEVSTVLYPGLKNHPGHEVAAKQMKRF
GGMISVRFAGGEEAAKKFCTSTKLICLAESLGGVESLLEHPATMTHQSAA
GSQLEVPRDLVRISIGIEDIEDLLADVEQALNNLH
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
5x5h Chain A Residue 405 [
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Receptor-Ligand Complex Structure
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PDB
5x5h
Structural Insights into Substrate Specificity of Cystathionine gamma-Synthase from Corynebacterium glutamicum
Resolution
1.51 Å
Binding residue
(original residue number in PDB)
E71 Q189 P190 L191
Binding residue
(residue number reindexed from 1)
E69 Q187 P188 L189
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
R54 Y107 D179 K204
Catalytic site (residue number reindexed from 1)
R52 Y105 D177 K202
Enzyme Commision number
2.5.1.48
: cystathionine gamma-synthase.
Gene Ontology
Molecular Function
GO:0003962
cystathionine gamma-synthase activity
GO:0016740
transferase activity
GO:0016846
carbon-sulfur lyase activity
GO:0030170
pyridoxal phosphate binding
GO:0046872
metal ion binding
Biological Process
GO:0009086
methionine biosynthetic 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:5x5h
,
PDBe:5x5h
,
PDBj:5x5h
PDBsum
5x5h
PubMed
28675039
UniProt
Q79VD9
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