Structure of PDB 5xj9 Chain A Binding Site BS01

Receptor Information
>5xj9 Chain A (length=200) Species: 224324 (Aquifex aeolicus VF5) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSALFLVIFAYLLGSITFGEVIAKLKGVDLRNVGSGNVGATNVTRALGKK
YGVLVFFLDFLKGFIPALIAVKSFGIDSWVLTFTGLASVLGHMYPVFFGF
KGGKGVATALGVVFAVSPSVALFSFLVWLGIFLWKRYVSLASITATISAF
LFLFVAGYPVNVLFMAIVIGALIIYRHRENINRLLTGREHRFGTLEVLFQ
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 chain5xj9 Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5xj9 Structural insights into the committed step of bacterial phospholipid biosynthesis.
Resolution1.83 Å
Binding residue
(original residue number in PDB)
K135 R136 R191
Binding residue
(residue number reindexed from 1)
K135 R136 R191
Annotation score1
Enzymatic activity
Enzyme Commision number 2.3.1.275: acyl phosphate:glycerol-3-phosphate acyltransferase.
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0043772 acyl-phosphate glycerol-3-phosphate acyltransferase activity
Biological Process
GO:0006644 phospholipid metabolic process
GO:0008654 phospholipid biosynthetic process
Cellular Component
GO:0005886 plasma membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5xj9, PDBe:5xj9, PDBj:5xj9
PDBsum5xj9
PubMed29167463
UniProtO66905|PLSY_AQUAE Glycerol-3-phosphate acyltransferase (Gene Name=plsY)

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