Structure of PDB 3gsh Chain A Binding Site BS02

Receptor Information
>3gsh Chain A (length=91) Species: 4513 (Hordeum vulgare) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LNCGQVDSKMKPCLTYVQGGPGPSGECCNGVRDLHNQAQSSGDRQTVCNC
LKGIARGIHNLNLNNAASIPSKCNVNVPYTISPDIDCSRIY
Ligand information
Ligand IDTFA
InChIInChI=1S/C2HF3O2/c3-2(4,5)1(6)7/h(H,6,7)
InChIKeyDTQVDTLACAAQTR-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01FC(F)(F)C(=O)O
CACTVS 3.370OC(=O)C(F)(F)F
OpenEye OEToolkits 1.7.0C(=O)(C(F)(F)F)O
FormulaC2 H F3 O2
Nametrifluoroacetic acid
ChEMBLCHEMBL506259
DrugBank
ZINCZINC000003860798
PDB chain3gsh Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3gsh The crystal structure of oxylipin-conjugated barley LTP1 highlights the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		L34 H35 V47 V77 P78
Binding residue
(residue number reindexed from 1)		L34 H35 V47 V77 P78
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Biological Process
GO:0006869 lipid transport
Cellular Component
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3gsh, PDBe:3gsh, PDBj:3gsh
PDBsum3gsh
PubMed19836358
UniProtP07597|NLTP1_HORVU Non-specific lipid-transfer protein 1 (Gene Name=LTP1)

[Back to BioLiP]