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- SASDDD6: Human Guanylate-binding protein (hGBP1) (Guanylate-binding protein 1) -

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Open data


ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDDD6
SampleHuman Guanylate-binding protein (hGBP1)
  • Guanylate-binding protein 1 (protein), Homo sapiens
Function / homology
Function and homology information


GDP phosphatase activity / non-canonical inflammasome complex assembly / negative regulation of substrate adhesion-dependent cell spreading / protein localization to vacuole / symbiont cell surface / cytolysis in another organism / positive regulation of pyroptotic inflammatory response / vesicle membrane / negative regulation of interleukin-2 production / negative regulation of T cell receptor signaling pathway ...GDP phosphatase activity / non-canonical inflammasome complex assembly / negative regulation of substrate adhesion-dependent cell spreading / protein localization to vacuole / symbiont cell surface / cytolysis in another organism / positive regulation of pyroptotic inflammatory response / vesicle membrane / negative regulation of interleukin-2 production / negative regulation of T cell receptor signaling pathway / spectrin binding / defense response to protozoan / cytokine binding / cellular response to interleukin-1 / negative regulation of protein localization to plasma membrane / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / regulation of protein localization to plasma membrane / regulation of calcium-mediated signaling / cytoplasmic vesicle membrane / Hsp90 protein binding / lipopolysaccharide binding / negative regulation of ERK1 and ERK2 cascade / cellular response to type II interferon / Interferon gamma signaling / cellular response to tumor necrosis factor / GDP binding / actin cytoskeleton / G protein activity / actin binding / cytoplasmic vesicle / defense response to virus / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / defense response to bacterium / Golgi membrane / innate immune response / GTPase activity / GTP binding / enzyme binding / Golgi apparatus / protein homodimerization activity / extracellular region / identical protein binding / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Guanylate-binding protein, C-terminal / Guanylate-binding protein/Atlastin, C-terminal / Guanylate-binding protein, C-terminal domain / Guanylate-binding protein, C-terminal domain superfamily / Guanylate-binding protein, N-terminal / Guanylate-binding protein, N-terminal domain / GB1/RHD3-type guanine nucleotide-binding (G) domain / GB1/RHD3-type guanine nucleotide-binding (G) domain profile. / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Guanylate-binding protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Contact author
  • Andreas Stadler (Forschungszentrum Jülich)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #1969
Type: dummy / Software: (2.7.1) / Radius of dummy atoms: 3.25 A / Chi-square value: 2.950
Search similar-shape structures of this assembly by Omokage search (details)
Model #1995
Type: dummy / Software: (2.8.3) / Radius of dummy atoms: 1.50 A / Chi-square value: 2.950
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Human Guanylate-binding protein (hGBP1) / Specimen concentration: 16.1 mg/ml
BufferName: 50 mM TRIS, 5 mM MgCl2, 150 mM NaCl / pH: 7.9
Entity #1063Type: protein / Description: Guanylate-binding protein 1 / Formula weight: 67.629 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P32455
Sequence: MASEIHMTGP MCLIENTNGR LMANPEALKI LSAITQPMVV VAIVGLYRTG KSYLMNKLAG KKKGFSLGST VQSHTKGIWM WCVPHPKKPG HILVLLDTEG LGDVEKGDNQ NDSWIFALAV LLSSTFVYNS IGTINQQAMD QLYYVTELTH RIRSKSSPDE NENEVEDSAD ...Sequence:
MASEIHMTGP MCLIENTNGR LMANPEALKI LSAITQPMVV VAIVGLYRTG KSYLMNKLAG KKKGFSLGST VQSHTKGIWM WCVPHPKKPG HILVLLDTEG LGDVEKGDNQ NDSWIFALAV LLSSTFVYNS IGTINQQAMD QLYYVTELTH RIRSKSSPDE NENEVEDSAD FVSFFPDFVW TLRDFSLDLE ADGQPLTPDE YLTYSLKLKK GTSQKDETFN LPRLCIRKFF PKKKCFVFDR PVHRRKLAQL EKLQDEELDP EFVQQVADFC SYIFSNSKTK TLSGGIQVNG PRLESLVLTY VNAISSGDLP CMENAVLALA QIENSAAVQK AIAHYEQQMG QKVQLPTETL QELLDLHRDS EREAIEVFIR SSFKDVDHLF QKELAAQLEK KRDDFCKQNQ EASSDRCSAL LQVIFSPLEE EVKAGIYSKP GGYRLFVQKL QDLKKKYYEE PRKGIQAEEI LQTYLKSKES MTDAILQTDQ TLTEKEKEIE VERVKAESAQ ASAKMLQEMQ RKNEQMMEQK ERSYQEHLKQ LTEKMENDRV QLLKEQERTL ALKLQEQEQL LKEGFQKESR IMKNEIQDLQ TKMRRRKAC

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Experimental information

BeamInstrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotron / Wavelength: 0.099 Å / Dist. spec. to detc.: 2.876 mm
DetectorName: Pilatus 1M
Scan
Title: Human Guanylate-binding protein (hGBP1) / Measurement date: Apr 30, 2018 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 114 / Unit: 1/nm /
MinMax
Q0.0606 4.9445
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 413 /
MinMax
Q0.173204 2.08788
P(R) point1 413
R0 14.4
Result
Type of curve: sec
Comments: Column type: Size exclusion chromatography (Superdex 200 10/300 GL, GE Healthcare) flow rate: 0.5 ml/min.
ExperimentalPorod
MW65.3 kDa66.1 kDa
Volume-104.9 nm3

P(R)GuinierGuinier error
Forward scattering, I066.1 65.9 0.06
Radius of gyration, Rg4.018 nm3.89 nm0.06

MinMax
D-14.4
Guinier point31 52

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