Structure of PDB 8cqb Chain B Binding Site BS02

Receptor Information
>8cqb Chain B (length=478) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLM
NKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVE
KGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSK
SSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYS
LKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQD
EELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAIS
SGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTETLQELLD
LHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSD
RCSALLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGI
QAEEILQTYLKSKESMTDAILQTDQTLT
Ligand information
Ligand IDAF3
InChIInChI=1S/Al.3FH/h;3*1H/q+3;;;/p-3
InChIKeyKLZUFWVZNOTSEM-UHFFFAOYSA-K
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		F[Al](F)F
FormulaAl F3
NameALUMINUM FLUORIDE
ChEMBL
DrugBank
ZINC
PDB chain8cqb Chain B Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB8cqb Cryo-EM structure of the human GBP1 dimer bound to GDP-AlF3
Resolution3.7 Å
Binding residue
(original residue number in PDB)		K51 S73 T75 G100
Binding residue
(residue number reindexed from 1)		K46 S68 T70 G95
Annotation score1
Enzymatic activity
Enzyme Commision number 3.6.1.-
3.6.5.-
Gene Ontology
Molecular Function
GO:0001530 lipopolysaccharide binding
GO:0003779 actin binding
GO:0003924 GTPase activity
GO:0003925 G protein activity
GO:0004382 GDP phosphatase activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0016787 hydrolase activity
GO:0019003 GDP binding
GO:0019899 enzyme binding
GO:0019955 cytokine binding
GO:0030507 spectrin binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0051879 Hsp90 protein binding
Biological Process
GO:0032703 negative regulation of interleukin-2 production
GO:0042742 defense response to bacterium
GO:0042832 defense response to protozoan
GO:0045087 innate immune response
GO:0050848 regulation of calcium-mediated signaling
GO:0050860 negative regulation of T cell receptor signaling pathway
GO:0051607 defense response to virus
GO:0051715 cytolysis in another organism
GO:0070373 negative regulation of ERK1 and ERK2 cascade
GO:0071346 cellular response to type II interferon
GO:0071347 cellular response to interleukin-1
GO:0071356 cellular response to tumor necrosis factor
GO:0072665 protein localization to vacuole
GO:0140639 positive regulation of pyroptotic inflammatory response
GO:0160075 non-canonical inflammasome complex assembly
GO:1900025 negative regulation of substrate adhesion-dependent cell spreading
GO:1903076 regulation of protein localization to plasma membrane
GO:1903077 negative regulation of protein localization to plasma membrane
Cellular Component
GO:0000139 Golgi membrane
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005794 Golgi apparatus
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0012506 vesicle membrane
GO:0015629 actin cytoskeleton
GO:0030659 cytoplasmic vesicle membrane
GO:0031410 cytoplasmic vesicle
GO:0106139 symbiont cell surface

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8cqb, PDBe:8cqb, PDBj:8cqb
PDBsum8cqb
PubMed
UniProtP32455|GBP1_HUMAN Guanylate-binding protein 1 (Gene Name=GBP1)

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