Structure of PDB 1lqk Chain A Binding Site BS01

Receptor Information
>1lqk Chain A (length=134) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLS
REPQYGGPAADYTHYAFGIAAADFARFAAQLRAHGVREWKQNRSEGDSFY
FLDPDGHRLEAHVGDLRSRLAACRQAPYAGMRFA
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain1lqk Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1lqk Crystal structure of a genomically encoded fosfomycin resistance protein (FosA) at 1.19 A resolution by MAD phasing off the L-III edge of Tl(+)
Resolution1.35 Å
Binding residue
(original residue number in PDB)		K90 Y100 E110 R119
Binding residue
(residue number reindexed from 1)		K90 Y100 E110 R119
Annotation score1
Enzymatic activity
Enzyme Commision number 2.5.1.18: glutathione transferase.
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0046677 response to antibiotic
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:1lqk, PDBe:1lqk, PDBj:1lqk
PDBsum1lqk
PubMed12224946
UniProtQ9I4K6|FOSA_PSEAE Glutathione transferase FosA (Gene Name=fosA)

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