Structure of PDB 7cqm Chain B Binding Site BS02

Receptor Information
>7cqm Chain B (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 IDSEY
InChIInChI=1S/CH4N2Se/c2-1(3)4/h(H4,2,3,4)
InChIKeyIYKVLICPFCEZOF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.370NC(N)=[Se]
OpenEye OEToolkits 1.7.6C(=[Se])(N)N
ACDLabs 12.01[Se]=C(N)N
FormulaC H4 N2 Se
Nameselenourea
ChEMBLCHEMBL3187603
DrugBank
ZINC
PDB chain7cqm Chain B Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7cqm Selenourea for experimental phasing of membrane protein crystals grown in lipid cubic phase
Resolution1.8 Å
Binding residue
(original residue number in PDB)		F154 G157 Y158
Binding residue
(residue number reindexed from 1)		F154 G157 Y158
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:7cqm, PDBe:7cqm, PDBj:7cqm
PDBsum7cqm
PubMed
UniProtO66905|PLSY_AQUAE Glycerol-3-phosphate acyltransferase (Gene Name=plsY)

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