9i5w

Structure of mature Activin A from DMSO solvent optimisation of XChem fragment screen

Method: X-RAY DIFFRACTION Dmax: 68.1 Å Quality: GOOD

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

Inhibin beta A chain

Homo sapiens

UniProt P08476

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 311–426 Chain B; UniProt 311–426 Not recorded DMS DIMETHYL SULFOXIDE × 6 SO4 SULFATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;294 K;1.55 M (NH4)2SO4, 100 mM Hepes pH 7.4, 8 % DMSO, 40 mM NaSO4 Resolution 1.77 Å R-free 0.235

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 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INHBA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–116; UniProt 311–426 Author chain B; PDBConstruct 1–116; UniProt 311–426

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 9i5w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9i5w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9i5w
Deposition date deposition_date2025-01-28
最后修订 last_revision2025-02-12
Structure title titleStructure of mature Activin A from DMSO solvent optimisation of XChem fragment screen
Keywords keywordsactivin A, TGF-beta, growth factor, FBDD, inhibitor, 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_guinier20.34
Radius of gyration Rg (electron density) rg_electron19.84
Forward intensity I(0) i014112200.00
Molecular weight molecular_weight26112.0 kDa
Excluded volume excluded_volume31827 ų
Envelope volume envelope_volume39802 ų
Hydration-shell volume shell_volume17556 ų
Envelope diameter envelope_diameter70.0
Shell Rg shell_rg25.37
Envelope Rg envelope_rg20.07
Shape Rg shape_rg19.94
Total Rg total_rg20.39
Total atoms total_atoms1806
Residues n_residues222
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 dmax68.1
Rg (real space) rg_real20.35
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.4110e+07
I(0) uncertainty (real space) i0_real_error1.7850e+05
Rg (reciprocal space) rg_reciprocal20.35
I(0) (reciprocal space) i0_reciprocal14110000.0000
Solution quality estimate total_estimate0.8054
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.381
Kurtosis Kurtosis kurtosis-0.237
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2263000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)