SASBDB entries for UniProt ID:

SASDKV7 – CCP2-SP domains of the complement C1r subcomponent

UniProt ID: P00736 (375-705) Complement C1r subcomponent
Complement C1r subcomponent experimental SAS data
PYMOL model
Sample: Complement C1r subcomponent monomer, 38 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 140 mM NaCl, pH: 7.3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 24
A Structural Basis for Inhibition of the Complement Initiator Protease C1r by Lyme Disease Spirochetes. J Immunol 207(11):2856-2867 (2021)
Garrigues RJ, Powell-Pierce AD, Hammel M, Skare JT, Garcia BL
RgGuinier 2.4 nm
Dmax 7.9 nm
VolumePorod 63 nm3

SASDKW7 – Complement inhibitory domain of the Borrelia burgdorferi fibronectin-binding protein BBK32

UniProt ID: O50835 (206-348) Fibronectin-binding protein BBK32
Fibronectin-binding protein BBK32 experimental SAS data
PYMOL model
Sample: Fibronectin-binding protein BBK32 monomer, 17 kDa Borreliella burgdorferi B31 protein
Buffer: 10 mM HEPES, 140 mM NaCl, pH: 7.3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 24
A Structural Basis for Inhibition of the Complement Initiator Protease C1r by Lyme Disease Spirochetes. J Immunol 207(11):2856-2867 (2021)
Garrigues RJ, Powell-Pierce AD, Hammel M, Skare JT, Garcia BL
RgGuinier 2.1 nm
Dmax 7.6 nm
VolumePorod 34 nm3

SASDKX7 – CCP2-SP domains of the complement C1r subcomponent bound to the complement inhibitory domain of the Borrelia burgdorferi fibronectin-binding protein BBK32

UniProt ID: O50835 (206-348) Fibronectin-binding protein BBK32

UniProt ID: P00736 (376-705) Complement C1r subcomponent
Fibronectin-binding protein BBK32Complement C1r subcomponent experimental SAS data
PYMOL model
Sample: Fibronectin-binding protein BBK32 monomer, 17 kDa Borrelia burgdorferi (strain … protein
Complement C1r subcomponent monomer, 38 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 140 mM NaCl, pH: 7.3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 24
A Structural Basis for Inhibition of the Complement Initiator Protease C1r by Lyme Disease Spirochetes. J Immunol 207(11):2856-2867 (2021)
Garrigues RJ, Powell-Pierce AD, Hammel M, Skare JT, Garcia BL
RgGuinier 2.8 nm
Dmax 8.6 nm
VolumePorod 75 nm3

SASDKY7 – α-L-Fucosidase isoenzyme 2 from Paenibacillus thiaminolyticus - wild type

UniProt ID: K0JCW6 (1-660) Alpha-L-fucosidase
Alpha-L-fucosidase experimental SAS data
OTHER model
Sample: Alpha-L-fucosidase tetramer, 297 kDa Paenibacillus thiaminolyticus (Bacillus … protein
Buffer: 50 mM potassium phosphate, pH: 7.4
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2019 Jul 16
The first structure–function study of GH151 α‐ l ‐fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity The FEBS Journal (2022)
Koval'ová T, Kovaľ T, Stránský J, Kolenko P, Dušková J, Švecová L, Vodičková P, Spiwok V, Benešová E, Lipovová P, Dohnálek J
RgGuinier 4.2 nm
Dmax 13.2 nm
VolumePorod 418 nm3

SASDKZ7 – α-L-Fucosidase isoenzyme 2 from Paenibacillus thiaminolyticus - mutant H503A

UniProt ID: K0JCW6 (1-660) Alpha-L-fucosidase H503A
Alpha-L-fucosidase H503A experimental SAS data
PYMOL model
Sample: Alpha-L-fucosidase H503A tetramer, 297 kDa Paenibacillus thiaminolyticus (Bacillus … protein
Buffer: 50 mM potassium phosphate, pH: 7.4
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2019 Jul 16
The first structure–function study of GH151 α‐ l ‐fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity The FEBS Journal (2022)
Koval'ová T, Kovaľ T, Stránský J, Kolenko P, Dušková J, Švecová L, Vodičková P, Spiwok V, Benešová E, Lipovová P, Dohnálek J
RgGuinier 4.5 nm
Dmax 13.5 nm
VolumePorod 433 nm3

SASDK48 – Histidine kinase AdeS - DHp-CA Domain

UniProt ID: Q93E22 (130-357) Histidine kinase
Histidine kinase experimental SAS data
MULTIFOXS model
Sample: Histidine kinase dimer, 51 kDa Acinetobacter baumannii protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2018 Apr 21
Proteolysis and multimerization regulate signaling along the two-component regulatory system AdeRS. iScience 24(5):102476 (2021)
Ouyang Z, Zheng F, Zhu L, Felix J, Wu D, Wu K, Gutsche I, Wu Y, Hwang PM, She J, Wen Y
RgGuinier 2.8 nm
Dmax 9.1 nm
VolumePorod 85 nm3

SASDK58 – Histidine kinase AdeS - cytoplasmic domain

UniProt ID: Q93E22 (84-357) Histidine kinase
Histidine kinase experimental SAS data
OTHER model
Sample: Histidine kinase hexamer, 186 kDa Acinetobacter baumannii protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 19
Proteolysis and multimerization regulate signaling along the two-component regulatory system AdeRS. iScience 24(5):102476 (2021)
Ouyang Z, Zheng F, Zhu L, Felix J, Wu D, Wu K, Gutsche I, Wu Y, Hwang PM, She J, Wen Y
RgGuinier 4.6 nm
Dmax 16.3 nm
VolumePorod 378 nm3

SASDK68 – Transcriptional intermediary factor 2 (TIF2) intrinsically disordered coactivator

UniProt ID: Q15596-1 (624-773) Nuclear receptor coactivator 2
Nuclear receptor coactivator 2 experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Nuclear receptor coactivator 2 monomer, 16 kDa Homo sapiens protein
Buffer: 150 mM NaCl, 50 mM BisTris pH 6.8, and 0.5 mM EDTA, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 14
Structural Insights into the Interaction of the Intrinsically Disordered Co-activator TIF2 with Retinoic Acid Receptor Heterodimer (RXR/RAR). J Mol Biol 433(9):166899 (2021)
Senicourt L, le Maire A, Allemand F, Carvalho JE, Guee L, Germain P, Schubert M, Bernadó P, Bourguet W, Sibille N
RgGuinier 3.7 nm
Dmax 16.3 nm
VolumePorod 50 nm3

SASDK78 – E3 ubiquitin/ISG15 ligase TRIM25, apo form (TRIM25 apo)

UniProt ID: Q14258 (189-630) E3 ubiquitin/ISG15 ligase TRIM25
E3 ubiquitin/ISG15 ligase TRIM25 experimental SAS data
E3 ubiquitin/ISG15 ligase TRIM25 Kratky plot
Sample: E3 ubiquitin/ISG15 ligase TRIM25 dimer, 100 kDa Homo sapiens protein
Buffer: 20 mM MES, 75 mM NaCl, 1 mM TCEP, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Nov 19
The molecular dissection of TRIM25's RNA-binding mechanism provides key insights into its antiviral activity. Nat Commun 15(1):8485 (2024)
Álvarez L, Haubrich K, Iselin L, Gillioz L, Ruscica V, Lapouge K, Augsten S, Huppertz I, Choudhury NR, Simon B, Masiewicz P, Lethier M, Cusack S, Rittinger K, Gabel F, Leitner A, Michlewski G, Hentze MW, Allain FHT, Castello A, Hennig J
RgGuinier 6.8 nm
Dmax 30.2 nm

SASDK88 – E3 ubiquitin/ISG15 ligase TRIM25 bound to pre-let-7-a-1@1 RNA (TRIM25/pre-let-7)

UniProt ID: Q14258 (189-630) E3 ubiquitin/ISG15 ligase TRIM25

UniProt ID: None (None-None) pre-let-7-a-1@1
E3 ubiquitin/ISG15 ligase TRIM25pre-let-7-a-1@1 experimental SAS data
E3 ubiquitin/ISG15 ligase TRIM25 pre-let-7-a-1@1 Kratky plot
Sample: E3 ubiquitin/ISG15 ligase TRIM25 dimer, 100 kDa Homo sapiens protein
Pre-let-7-a-1@1 monomer, 9 kDa synthetic construct RNA
Buffer: 20 mM MES, 75 mM NaCl, 1 mM TCEP, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 14
The molecular dissection of TRIM25's RNA-binding mechanism provides key insights into its antiviral activity. Nat Commun 15(1):8485 (2024)
Álvarez L, Haubrich K, Iselin L, Gillioz L, Ruscica V, Lapouge K, Augsten S, Huppertz I, Choudhury NR, Simon B, Masiewicz P, Lethier M, Cusack S, Rittinger K, Gabel F, Leitner A, Michlewski G, Hentze MW, Allain FHT, Castello A, Hennig J
RgGuinier 5.7 nm
Dmax 19.8 nm