8bwm

Crystal structure of human Twisted gastrulation protein homolog 1 (TWSG1) in complex with human Growth Differentiation factor 5 (GDF5) and calcium, long-wavelength X-ray dataset (4042 eV)

Method: X-RAY DIFFRACTION Dmax: 75.3 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Growth/differentiation factor 5

Homo sapiens

UniProt P43026

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 382–501 Chain B; UniProt 382–501 Not recorded Twisted gastrulation protein homolog 1 × 2 (Q9GZX9) CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;12.1% w/v PEG 1000, 12.1% w/v PEG 3350, 12.1% v/v MPD, 97 mM CaCl2, 0.097 M Bicine/Trizma pH 8.5 Resolution 2.50 Å R-free 0.278

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

14 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GDF5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–121; UniProt 382–501 Author chain B; PDBConstruct 2–121; UniProt 382–501

Twisted gastrulation protein homolog 1

Homo sapiens

UniProt Q9GZX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 26–83 Chain D; UniProt 26–83 Not recorded Growth/differentiation factor 5 × 2 (P43026) CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;12.1% w/v PEG 1000, 12.1% w/v PEG 3350, 12.1% v/v MPD, 97 mM CaCl2, 0.097 M Bicine/Trizma pH 8.5 Resolution 2.50 Å R-free 0.278

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TWSG1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 4–61; UniProt 26–83 Author chain D; PDBConstruct 4–61; UniProt 26–83

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8bwm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8bwm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8bwm
Deposition date deposition_date2022-12-07
Structure title titleCrystal structure of human Twisted gastrulation protein homolog 1 (TWSG1) in complex with human Growth Differentiation factor 5 (GDF5) and calcium, long-wavelength X-ray dataset (4042 eV)
Keywords keywords;Twisted gastrulation protein homolog 1 (TWSG1), Growth Differentiation factor 5 (GDF5), Transforming Growth Factor beta (TGF-beta) signalling pathway, long-wavelength X-rays., SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier22.99
Radius of gyration Rg (electron density) rg_electron22.61
Forward intensity I(0) i023467100.00
Molecular weight molecular_weight34614.0 kDa
Excluded volume excluded_volume42311 ų
Envelope volume envelope_volume52129 ų
Hydration-shell volume shell_volume20059 ų
Envelope diameter envelope_diameter75.5
Shell Rg shell_rg28.50
Envelope Rg envelope_rg22.76
Shape Rg shape_rg22.58
Total Rg total_rg23.41
Total atoms total_atoms4598
Residues n_residues309
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax75.3
Rg (real space) rg_real23.10
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real2.3470e+07
I(0) uncertainty (real space) i0_real_error3.3340e+05
Rg (reciprocal space) rg_reciprocal23.07
I(0) (reciprocal space) i0_reciprocal23470000.0000
Solution quality estimate total_estimate0.8771
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.2
Skewness Skewness skewness0.454
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4430000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.831; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.927; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)