SASBDB entries for UniProt ID:

SASDVD7 – Regulatory domain of L-threonine dehydratase biosynthetic IlvA (EcIlvA) from Eschericia coli

UniProt ID: P04968 (335-514) L-threonine dehydratase biosynthetic IlvA Regulatory domain
L-threonine dehydratase biosynthetic IlvA Regulatory domain experimental SAS data
CHIMERA model
Sample: L-threonine dehydratase biosynthetic IlvA Regulatory domain dimer, 46 kDa Escherichia coli (strain … protein
Buffer: 20 mM KPO4, 200 mM NaCl, 0.1 mM TCEP,, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Oct 14
Isoleucine Binding and Regulation of Escherichia coli and Staphylococcus aureus Threonine Dehydratase (IlvA). Biochemistry (2025)
Yun MK, Subramanian C, Miller K, Jackson P, Radka CD, Rock CO
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 50 nm3

SASDVE7 – Hexameric L-threonine dehydratase biosynthetic (IlvA) from Staphylococcus aureus

UniProt ID: Q2FF63 (336-422) L-threonine dehydratase biosynthetic IlvA
L-threonine dehydratase biosynthetic IlvA experimental SAS data
CHIMERA model
Sample: L-threonine dehydratase biosynthetic IlvA hexamer, 288 kDa Staphylococcus aureus (strain … protein
Buffer: 20 mM KPO4, 200 mM NaCl, 0.1 mM TCEP,, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Oct 14
Isoleucine Binding and Regulation of Escherichia coli and Staphylococcus aureus Threonine Dehydratase (IlvA). Biochemistry (2025)
Yun MK, Subramanian C, Miller K, Jackson P, Radka CD, Rock CO
RgGuinier 5.1 nm
Dmax 17.1 nm
VolumePorod 386 nm3

SASDVF7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (ADAR1) (residues 688-817, i.e. dsRBD3-long)

UniProt ID: P55265 (688-817) Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long)
Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long) experimental SAS data
Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long) Kratky plot
Sample: Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long) dimer, 29 kDa Homo sapiens protein
Buffer: 20 mM Na-HEPES, 55 mM KOAc, 10 mM NaCl, 1 mM TCEP, pH: 7.3
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Jun 27
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 2.6 nm
Dmax 8.0 nm
VolumePorod 50 nm3

SASDVG7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (ADAR1) (residues 708-801, i.e. dsRBD3-mid)

UniProt ID: P55265 (708-801) Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid)
Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid) experimental SAS data
Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid) Kratky plot
Sample: Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid) dimer, 22 kDa Homo sapiens protein
Buffer: 20 mM Na-HEPES, 55 mM KOAc, 10 mM NaCl, 1 mM TCEP, pH: 7.3
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Jun 27
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 2.0 nm
Dmax 6.7 nm
VolumePorod 27 nm3

SASDVH7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (ADAR1) (residues 716-797, i.e. dsRBD3-short)

UniProt ID: P55265 (716-797) Third double-stranded RNA-binding domain of human ADAR1 (residues 716-797, i.e. dsRBD3-short)
Third double-stranded RNA-binding domain of human ADAR1 (residues 716-797, i.e. dsRBD3-short) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Third double-stranded RNA-binding domain of human ADAR1 (residues 716-797, i.e. dsRBD3-short) dimer, 18 kDa Homo sapiens protein
Buffer: 20 mM Na-HEPES, 55 mM KOAc, 10 mM NaCl, 1 mM TCEP, pH: 7.3
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Jun 27
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 1.9 nm
Dmax 5.5 nm
VolumePorod 27 nm3

SASDVJ7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (ADAR1) (wild-type, residues 708-801, i.e. ADAR1-dsRBD3)

UniProt ID: P55265 (708-801) Third double-stranded RNA-binding domain of human ADAR1 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3)
Third double-stranded RNA-binding domain of human ADAR1 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3) experimental SAS data
Third double-stranded RNA-binding domain of human ADAR1 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3) Kratky plot
Sample: Third double-stranded RNA-binding domain of human ADAR1 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3) dimer, 25 kDa Homo sapiens protein
Buffer: 20 mM Na-phosphate, 100 mM NaCl, 2 mM 2-mercaptoethanol, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2021 Oct 8
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 2.4 nm
Dmax 9.1 nm
VolumePorod 39 nm3

SASDVK7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant)

UniProt ID: P55265 (708-801) Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant)
Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) experimental SAS data
Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) Kratky plot
Sample: Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) monomer, 12 kDa Homo sapiens protein
Buffer: 20 mM Na-phosphate, 100 mM NaCl, 2 mM 2-mercaptoethanol, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2021 Oct 8
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 2.1 nm
Dmax 7.2 nm
VolumePorod 20 nm3

SASDVL7 – Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2)

UniProt ID: P55265 (708-801) Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2)
Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) experimental SAS data
Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) Kratky plot
Sample: Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) monomer, 13 kDa Homo sapiens / … protein
Buffer: 20 mM Na-phosphate, 100 mM NaCl, 2 mM 2-mercaptoethanol, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2021 Oct 8
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 2.0 nm
Dmax 6.4 nm
VolumePorod 16 nm3

SASDVS7 – Cadherin EGF LAG seven-pass G-type receptor 1 (CELSR1) ECR without calcium

UniProt ID: O35161 (255-2477) Cadherin EGF LAG seven-pass G-type receptor 1
Cadherin EGF LAG seven-pass G-type receptor 1 experimental SAS data
Cadherin EGF LAG seven-pass G-type receptor 1 Kratky plot
Sample: Cadherin EGF LAG seven-pass G-type receptor 1 monomer, 245 kDa Mus musculus protein
Buffer: 10 mM Tris, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Dec 8
Structural basis for regulation of CELSR1 by a compact module in its extracellular region. Nat Commun 16(1):3972 (2025)
Bandekar SJ, Garbett K, Kordon SP, Dintzner EE, Li J, Shearer T, Sando RC, Araç D
RgGuinier 6.0 nm
Dmax 22.5 nm
VolumePorod 473 nm3

SASDVT7 – Cadherin EGF LAG seven-pass G-type receptor 1 (CELSR1) ECR with calcium

UniProt ID: O35161 (255-2477) Cadherin EGF LAG seven-pass G-type receptor 1
Cadherin EGF LAG seven-pass G-type receptor 1 experimental SAS data
Cadherin EGF LAG seven-pass G-type receptor 1 Kratky plot
Sample: Cadherin EGF LAG seven-pass G-type receptor 1 dimer, 491 kDa Mus musculus protein
Buffer: 10 mM Tris, 150 mM NaCl, 1 mM CaCl2, pH: 8.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Dec 8
Structural basis for regulation of CELSR1 by a compact module in its extracellular region. Nat Commun 16(1):3972 (2025)
Bandekar SJ, Garbett K, Kordon SP, Dintzner EE, Li J, Shearer T, Sando RC, Araç D
RgGuinier 16.2 nm
Dmax 67.5 nm
VolumePorod 722 nm3