Structure of PDB 8i09 Chain F Binding Site BS04

Receptor Information
>8i09 Chain F (length=245) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
CEELEIVWKNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANK
LASPIMPAIAIREVVEEAYAADPEMIASAACDIQAVRTRDPAVDKYSTPL
LYLKGFHALQAYRIGHWLWNKGRRALAIFLQNQVSVSFQVDIHPAAKIGR
GIMLDHATGIVVGETAVIEDDVSILQSVTLGGTGKTSGDRHPKIREGVMI
GAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGKP
Ligand information
Ligand IDCYS
InChIInChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
InChIKeyXUJNEKJLAYXESH-REOHCLBHSA-N
SMILES
SoftwareSMILES
CACTVS 3.341N[CH](CS)C(O)=O
OpenEye OEToolkits 1.5.0C([C@@H](C(=O)O)N)S
CACTVS 3.341N[C@@H](CS)C(O)=O
ACDLabs 10.04O=C(O)C(N)CS
OpenEye OEToolkits 1.5.0C(C(C(=O)O)N)S
FormulaC3 H7 N O2 S
NameCYSTEINE
ChEMBLCHEMBL863
DrugBankDB00151
ZINCZINC000000895042
PDB chain8i09 Chain F Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8i09 Alkyl gallates inhibit serine O -acetyltransferase in bacteria and enhance susceptibility of drug-resistant Gram-negative bacteria to antibiotics.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		D157 H158
Binding residue
(residue number reindexed from 1)		D155 H156
Annotation score2
Enzymatic activity
Enzyme Commision number 2.3.1.30: serine O-acetyltransferase.
Gene Ontology
Molecular Function
GO:0009001 serine O-acetyltransferase activity
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0006535 cysteine biosynthetic process from serine
GO:0008652 amino acid biosynthetic process
GO:0019344 cysteine biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8i09, PDBe:8i09, PDBj:8i09
PDBsum8i09
PubMed37965540
UniProtA0A0D6I3Y9

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