Structure of PDB 8r1a Chain F

Receptor sequence
>8r1aF (length=587) Species: 9606 (Homo sapiens) [Search protein sequence]
IHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYL
MNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDV
EKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRS
KSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTY
SLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQ
DEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAI
SSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTESLQELL
DLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASS
DRCSGLLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKG
IQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAK
MLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKL
QEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTI
3D structure
PDB8r1a Elucidating the activation mechanism for GBP1 oligomerization
ChainF
Resolution26.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.6.1.-
3.6.5.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 AF3 F Y47 R48 K51 T75 G100 Y43 R44 K47 T71 G96
BS02 MG F S52 T75 S48 T71
BS03 GDP F R48 G50 K51 S52 Y53 L67 G68 S69 R183 D184 L247 R44 G46 K47 S48 Y49 L63 G64 S65 R179 D180 L243
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:8r1a, PDBe:8r1a, PDBj:8r1a
PDBsum8r1a
PubMed38267655
UniProtP32455|GBP1_HUMAN Guanylate-binding protein 1 (Gene Name=GBP1)

[Back to BioLiP]