SASBDB entries for UniProt ID:

SASDWH3 – Thomasclavelia ramosa immunoglobulin A protease N-terminal domain

UniProt ID: Q9AES2 (31-313) IgA protease
IgA protease experimental SAS data
ALPHAFOLD model
Sample: IgA protease monomer, 32 kDa Thomasclavelia ramosa protein
Buffer: 25 mM HEPES, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2023 Jun 26
Structure of the Thomasclavelia ramosa immunoglobulin A protease reveals a modular and minimizable architecture distinct from other immunoglobulin A proteases. Proc Natl Acad Sci U S A 122(35):e2503549122 (2025)
Tran N, Frenette A, Holyoak T
RgGuinier 1.9 nm
Dmax 6.0 nm
VolumePorod 38 nm3

SASDWJ3 – Thomasclavelia ramosa immunoglobulin A protease middle (protease) domain

UniProt ID: Q9AES2 (329-807) IgA protease
IgA protease experimental SAS data
ALPHAFOLD model
Sample: IgA protease monomer, 55 kDa Thomasclavelia ramosa protein
Buffer: 25 mM HEPES, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2023 Jun 26
Structure of the Thomasclavelia ramosa immunoglobulin A protease reveals a modular and minimizable architecture distinct from other immunoglobulin A proteases. Proc Natl Acad Sci U S A 122(35):e2503549122 (2025)
Tran N, Frenette A, Holyoak T
RgGuinier 2.6 nm
Dmax 8.8 nm
VolumePorod 82 nm3

SASDWK3 – Thomasclavelia ramosa immunoglobulin A protease middle domain with C-terminal domain #1

UniProt ID: Q9AES2 (329-876) IgA protease
IgA protease experimental SAS data
PHENIX model
Sample: IgA protease monomer, 63 kDa Thomasclavelia ramosa protein
Buffer: 25 mM HEPES, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2023 Jun 26
Structure of the Thomasclavelia ramosa immunoglobulin A protease reveals a modular and minimizable architecture distinct from other immunoglobulin A proteases. Proc Natl Acad Sci U S A 122(35):e2503549122 (2025)
Tran N, Frenette A, Holyoak T
RgGuinier 2.7 nm
Dmax 9.2 nm
VolumePorod 89 nm3

SASDWL3 – Thomasclavelia ramosa immunoglobulin A protease C-terminal domain #2

UniProt ID: Q9AES2 (880-1008) IgA protease
IgA protease experimental SAS data
ALPHAFOLD model
Sample: IgA protease monomer, 14 kDa Thomasclavelia ramosa protein
Buffer: 25 mM HEPES, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2023 Jun 26
Structure of the Thomasclavelia ramosa immunoglobulin A protease reveals a modular and minimizable architecture distinct from other immunoglobulin A proteases. Proc Natl Acad Sci U S A 122(35):e2503549122 (2025)
Tran N, Frenette A, Holyoak T
RgGuinier 2.5 nm
Dmax 9.6 nm
VolumePorod 12 nm3

SASDWM3 – Thomasclavelia ramosa immunoglobulin A protease N-terminal domain with middle (protease) domain

UniProt ID: Q9AES2 (31-807) IgA protease
IgA protease experimental SAS data
CORAL model
Sample: IgA protease monomer, 88 kDa Thomasclavelia ramosa protein
Buffer: 25 mM HEPES, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2023 Jun 26
Structure of the Thomasclavelia ramosa immunoglobulin A protease reveals a modular and minimizable architecture distinct from other immunoglobulin A proteases. Proc Natl Acad Sci U S A 122(35):e2503549122 (2025)
Tran N, Frenette A, Holyoak T
RgGuinier 3.3 nm
Dmax 10.8 nm
VolumePorod 108 nm3

SASDWN3 – Thomasclavelia ramosa immunoglobulin A protease C-terminal tail

UniProt ID: Q9AES2 (808-1170) IgA protease
IgA protease experimental SAS data
CORAL model
Sample: IgA protease monomer, 39 kDa Thomasclavelia ramosa protein
Buffer: 25 mM HEPES, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2023 Jun 26
Structure of the Thomasclavelia ramosa immunoglobulin A protease reveals a modular and minimizable architecture distinct from other immunoglobulin A proteases. Proc Natl Acad Sci U S A 122(35):e2503549122 (2025)
Tran N, Frenette A, Holyoak T
RgGuinier 5.3 nm
Dmax 21.5 nm
VolumePorod 52 nm3

SASDWP3 – Thomasclavelia ramosa immunoglobulin A protease middle (protease) domain with C-terminal tail

UniProt ID: Q9AES2 (329-1170) IgA protease
IgA protease experimental SAS data
CORAL model
Sample: IgA protease monomer, 95 kDa Thomasclavelia ramosa protein
Buffer: 25 mM HEPES, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2023 Jun 26
Structure of the Thomasclavelia ramosa immunoglobulin A protease reveals a modular and minimizable architecture distinct from other immunoglobulin A proteases. Proc Natl Acad Sci U S A 122(35):e2503549122 (2025)
Tran N, Frenette A, Holyoak T
RgGuinier 5.7 nm
Dmax 24.0 nm
VolumePorod 160 nm3

SASDWQ3 – Thomasclavelia ramosa full-length immunoglobulin A protease

UniProt ID: Q9AES2 (31-1195) IgA protease
IgA protease experimental SAS data
CORAL model
Sample: IgA protease monomer, 131 kDa Thomasclavelia ramosa protein
Buffer: 25 mM HEPES, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2023 Jun 26
Structure of the Thomasclavelia ramosa immunoglobulin A protease reveals a modular and minimizable architecture distinct from other immunoglobulin A proteases. Proc Natl Acad Sci U S A 122(35):e2503549122 (2025)
Tran N, Frenette A, Holyoak T
RgGuinier 5.5 nm
Dmax 24.5 nm
VolumePorod 188 nm3

SASDW74 – Aromatic-L-amino-acid decarboxylase L353P bound to pyridoxal 5'-phosphate (PLP)

UniProt ID: P20711 (1-478) Aromatic-L-amino-acid decarboxylase (L353P)
Aromatic-L-amino-acid decarboxylase (L353P) experimental SAS data
DAMMIN model
Sample: Aromatic-L-amino-acid decarboxylase (L353P) dimer, 107 kDa Homo sapiens protein
Buffer: 50 mM HEPES, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2021 Jul 7
The CRISPR-Cas9 knockout DDC SH-SY5Y in vitro model for AADC deficiency provides insight into the pathogenicity of R347Q and L353P variants: a cross-sectional structural and functional analysis. FEBS J (2025)
Carmona-Carmona CA, Bisello G, Franchini R, Lunardi G, Galavotti R, Perduca M, Ribeiro RP, Belviso BD, Giorgetti A, Caliandro R, Lievens PM, Bertoldi M
RgGuinier 3.1 nm
Dmax 8.8 nm
VolumePorod 152 nm3

SASDW84 – Aromatic-L-amino-acid decarboxylase R347Q bound to pyridoxal 5'-phosphate (PLP)

UniProt ID: P20711 (1-478) Aromatic-L-amino-acid decarboxylase (R347Q)
Aromatic-L-amino-acid decarboxylase (R347Q) experimental SAS data
DAMMIN model
Sample: Aromatic-L-amino-acid decarboxylase (R347Q) dimer, 108 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 100 µM pyridoxal 5'-phosphate, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2021 Jul 7
The CRISPR-Cas9 knockout DDC SH-SY5Y in vitro model for AADC deficiency provides insight into the pathogenicity of R347Q and L353P variants: a cross-sectional structural and functional analysis. FEBS J (2025)
Carmona-Carmona CA, Bisello G, Franchini R, Lunardi G, Galavotti R, Perduca M, Ribeiro RP, Belviso BD, Giorgetti A, Caliandro R, Lievens PM, Bertoldi M
RgGuinier 3.6 nm
Dmax 14.2 nm
VolumePorod 220 nm3