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- EMDB-78199: Sterile alpha motif domain-containing protein 9, residues 623-1589 -

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Basic information

Entry
Database: EMDB / ID: EMD-78199
TitleSterile alpha motif domain-containing protein 9, residues 623-1589
Map data
Sample
  • Complex: SAMD9
    • Protein or peptide: Sterile alpha motif domain-containing protein 9
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
Keywordsinflammasome / signal transductionATPases with numerous domains (STAND) / sterile alpha motif. poxvirusrestriction factor / ANTIVIRAL PROTEIN / IMMUNE SYSTEM
Function / homology
Function and homology information


endosomal vesicle fusion / innate immune response / cytosol / cytoplasm
Similarity search - Function
SAM domain (Sterile alpha motif) / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Sterile alpha motif domain-containing protein 9
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsMou Z / Zhang F / Dai X / Xiang Y
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)Al151638 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM151043 United States
CitationJournal: To Be Published
Title: Sterile alpha motif domain-containing protein 9, residues 623-1589
Authors: Mou Z / Zhang F / Dai X / Xiang Y
History
DepositionJul 21, 2026-
Header (metadata) releaseAug 12, 2026-
Map releaseAug 12, 2026-
UpdateAug 12, 2026-
Current statusAug 12, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_78199.png

Downloads & links

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Map

FileDownload / File: emd_78199.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.66 Å/pix.
x 512 pix.
= 337.92 Å		0.66 Å/pix.
x 512 pix.
= 337.92 Å		0.66 Å/pix.
x 512 pix.
= 337.92 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.66 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.25
Minimum - Maximum-1.4057326 - 2.3043182
Average (Standard dev.)-0.00031061552 (±0.035956908)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 337.92 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_78199_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_78199_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : SAMD9

EntireName: SAMD9
Components
  • Complex: SAMD9
    • Protein or peptide: Sterile alpha motif domain-containing protein 9
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION

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Supramolecule #1: SAMD9

SupramoleculeName: SAMD9 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 110 KDa

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Macromolecule #1: Sterile alpha motif domain-containing protein 9

MacromoleculeName: Sterile alpha motif domain-containing protein 9 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 112.383867 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: SVTQSSKRLL PSIGLSTVLL KKEEDIMTAL EIICENECEG TLLEKDKNKF LEFKASKEED FYRGGKVSWW NFYFSSESYS SPFVKRDKY ERLEAMIQNC ADSSKPTSTK IIHLYHHPGC GGTTLAMHIL WELRKKFRCA VLKNKTVDFS EIGEQVTSLI T YGAMNRQE ...String:
SVTQSSKRLL PSIGLSTVLL KKEEDIMTAL EIICENECEG TLLEKDKNKF LEFKASKEED FYRGGKVSWW NFYFSSESYS SPFVKRDKY ERLEAMIQNC ADSSKPTSTK IIHLYHHPGC GGTTLAMHIL WELRKKFRCA VLKNKTVDFS EIGEQVTSLI T YGAMNRQE YVPVLLLVDD FEEQDNVYLL QYSIQTAIAK KYIRYEKPLV IILNCMRSQN PEKSARIPDS IAVIQQLSPK EQ RAFELKL KEIKEQHKNF EDFYSFMIMK TNFNKEYIEN VVRNILKGQN IFTKEAKLFS FLALLNSYVP DTTISLSQCE KFL GIGNKK AFWGTEKFED KMGTYSTILI KTEVIECGNY CGVRIIHSLI AEFSLEELKK SYHLNKSQIM LDMLTENLFF DTGM GKSKF LQDMHTLLLT RHRDEHEGET GNWFSPFIEA LHKDEGNEAV EAVLLESIHR FNPNAFICQA LARHFYIKKK DFGNA LNWA KQAKIIEPDN SYISDTLGQV YKSKIRWWIE ENGGNGNISV DDLIALLDLA EHASSAFKES QQQSEDREYE VKERLY PKS KRRYDTYNIA GYQGEIEVGL YTIQILQLIP FFDNKNELSK RYMVNFVSGS SDIPGDPNNE YKLALKNYIP YLTKLKF SL KKSFDFFDEY FVLLKPRNNI KQNEEAKTRR KVAGYFKKYV DIFCLLEESQ NNTGLGSKFS EPLQVERCRR NLVALKAD K FSGLLEYLIK SQEDAISTMK CIVNEYTFLL EQCTVKIQSK EKLNFILANI ILSCIQPTSR LVKPVEKLKD QLREVLQPI GLTYQFSEPY FLASLLFWPE NQQLDQHSEQ MKEYAQALKN SFKGQYKHMH RTKQPIAYFF LGKGKRLERL VHKGKIDQCF KKTPDINSL WQSGDVWKEE KVQELLLRLQ GRAENNCLYI EYGINEKITI PITPAFLGQL RSGRSIEKVS FYLGFSIGGP L AYDIEIV

UniProtKB: Sterile alpha motif domain-containing protein 9

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Macromolecule #2: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Macromolecule #3: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration1 mg/mL
BufferpH: 7.4
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 130000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 108548
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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