SAXSdb — 2b0u

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

Inhibin beta A chain

Homo sapiens

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 311–426 Chain B； UniProt 311–426	Fragment：Activin (mature form)	Follistatin × 2 （P19883） IR3 IRIDIUM (III) ION × 5 MLI MALONATE ION × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；PEG 3350, 200 mM Malonate, pH 7.0, vapor diffusion, hanging drop, temperature 295K	Resolution 2.80 Å R-free 0.297

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.

Other PDB	Difference from Current Entry 2B0U	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1NYS Crystal Structure of Activin A Bound to the ECD of ActRIIB P41 Deposited 2003-02-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 311–426（116 aa） Fragment：Mature Domain (residues 311-426) Chain D 311–426（116 aa） Fragment：Mature Domain (residues 311-426)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；PEG 4000, sodium chloride, hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 3.05 Å R-free 0.299
1NYU Crystal Structure of Activin A Bound to the ECD of ActRIIB Deposited 2003-02-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 311–426（116 aa） Fragment：Mature Domain (residues 311-426) Chain D 311–426（116 aa） Fragment：Mature Domain (residues 311-426)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；PEG 4000, sodium chloride, hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 3.10 Å R-free 0.291
1S4Y Crystal structure of the activin/actrIIb extracellular domain Deposited 2004-01-19	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 311–426（116 aa） Chain D 311–426（116 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.7；277 K；PEG 3350, magnesium chloride, bis tris, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.30 Å R-free 0.286
2ARP Activin A in complex with Fs12 fragment of follistatin Deposited 2005-08-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 311–426（116 aa）	Not recorded	NI NICKEL (II) ION × 6 1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL × 2 GOL GLYCEROL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；PEG-MME 2000, Nickel chloride, Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.254
2ARV Structure of human Activin A Deposited 2005-08-22	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 311–426（116 aa） Chain B 311–426（116 aa）	Not recorded	SO4 SULFATE ION × 4 GOL GLYCEROL × 3 1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；Ammonium sulphate, PEG300, Na-Hepes, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.259
2P6A The structure of the Activin:Follistatin 315 complex Deposited 2007-03-16	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 311–426（116 aa） Chain B 311–426（116 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；20-23% PEG 1000, 200mM MgCl2, 3% EtOH, 20mM Trimethyl-amine HCl, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298 K	Resolution 3.40 Å R-free 0.324
3B4V X-Ray structure of Activin in complex with FSTL3 Deposited 2007-10-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 311–426（116 aa） Chain B 311–426（116 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 2 SO4 SULFATE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEG 3350, ammonium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.48 Å R-free 0.279
3B4V X-Ray structure of Activin in complex with FSTL3 Deposited 2007-10-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 311–426（116 aa） Chain F 311–426（116 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEG 3350, ammonium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.48 Å R-free 0.279
5HLY Structure of Pro-Activin A Precursor at 2.3 A Resolution Deposited 2016-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 30–426（397 aa）	Mutation：C35S, C38S, deletion:K259-D282 Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；292 K；25% w/v polyethylene glycol 1000, 100 mM MES pH 6.5; cryo: 15% v/v PEG 400 added	Resolution 2.30 Å R-free 0.252
5HLZ Structure of Pro-Activin A Complex at 2.85 A resolution Deposited 2016-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 30–305（276 aa） Fragment：Pro domain, UNP Residues 30-305 Chain B 311–426（116 aa） Fragment：Mature domain, UNP Residues 311-426 Chain C 30–305（276 aa） Fragment：Pro domain, UNP Residues 30-305 Chain D 311–426（116 aa） Fragment：Mature domain, UNP Residues 311-426	Mutation：;C35S, C38S, deletion of K259-D282, furin cleavage site (RRRRR) replaced by HRV 3C protease cleavage site (LEVLFQGP),C35S, C38S, deletion of K259-D282, furin cleavage site replaced by HRV 3C protease cleavage site (LEVLFQGP),C35S, C38S, deletion of K259-D282, furin cleavage site (RRRRR) replaced by HRV 3C protease cleavage site (LEVLFQGP),C35S, C38S, deletion of K259-D282, furin cleavage site replaced by HRV 3C protease cleavage site (LEVLFQGP) ; Mutation：;C35S, C38S, deletion of K259-D282, furin cleavage site (RRRRR) replaced by HRV 3C protease cleavage site (LEVLFQGP),C35S, C38S, deletion of K259-D282, furin cleavage site replaced by HRV 3C protease cleavage site (LEVLFQGP),C35S, C38S, deletion of K259-D282, furin cleavage site (RRRRR) replaced by HRV 3C protease cleavage site (LEVLFQGP),C35S, C38S, deletion of K259-D282, furin cleavage site replaced by HRV 3C protease cleavage site (LEVLFQGP) ;	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；292 K；20% w/v polyethylene glycol 3350, 0.2 M calcium chloride; cryo: 15% v/v PEG 400 added	Resolution 2.85 Å R-free 0.274
5HLZ Structure of Pro-Activin A Complex at 2.85 A resolution Deposited 2016-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 30–305（276 aa） Fragment：Pro domain, UNP Residues 30-305 Chain F 311–426（116 aa） Fragment：Mature domain, UNP Residues 311-426 Chain G 30–305（276 aa） Fragment：Pro domain, UNP Residues 30-305 Chain H 311–426（116 aa） Fragment：Mature domain, UNP Residues 311-426	Mutation：;C35S, C38S, deletion of K259-D282, furin cleavage site (RRRRR) replaced by HRV 3C protease cleavage site (LEVLFQGP),C35S, C38S, deletion of K259-D282, furin cleavage site replaced by HRV 3C protease cleavage site (LEVLFQGP),C35S, C38S, deletion of K259-D282, furin cleavage site (RRRRR) replaced by HRV 3C protease cleavage site (LEVLFQGP),C35S, C38S, deletion of K259-D282, furin cleavage site replaced by HRV 3C protease cleavage site (LEVLFQGP) ; Mutation：;C35S, C38S, deletion of K259-D282, furin cleavage site (RRRRR) replaced by HRV 3C protease cleavage site (LEVLFQGP),C35S, C38S, deletion of K259-D282, furin cleavage site replaced by HRV 3C protease cleavage site (LEVLFQGP),C35S, C38S, deletion of K259-D282, furin cleavage site (RRRRR) replaced by HRV 3C protease cleavage site (LEVLFQGP),C35S, C38S, deletion of K259-D282, furin cleavage site replaced by HRV 3C protease cleavage site (LEVLFQGP) ;	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；292 K；20% w/v polyethylene glycol 3350, 0.2 M calcium chloride; cryo: 15% v/v PEG 400 added	Resolution 2.85 Å R-free 0.274
6Y6N Structure of mature activin A with small molecule 2 Deposited 2020-02-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 311–426（116 aa） Chain B 311–426（116 aa）	Not recorded	ODQ (3~{R})-3,4-dimethyl-3-propyl-1~{H}-1,4-benzodiazepine-2,5-dione × 1 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；291 K；1.65 M (NH4)2SO4, 4 % PEG 300, 100 mM Hepes pH 7.4, 2 % DMSO	Resolution 2.03 Å R-free 0.251
6Y6O Structure of mature activin A with small molecule 42 Deposited 2020-02-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 311–426（116 aa） Chain B 311–426（116 aa）	Not recorded	SO4 SULFATE ION × 10 OCK (3~{R})-4-ethyl-3-methyl-3-propyl-1~{H}-1,4-benzodiazepine-2,5-dione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；291 K；1.65 M (NH4)2SO4, 4 % PEG 300, 100 mM Hepes pH 7.4, 2 % DMSO	Resolution 2.04 Å R-free 0.254
7OLY Structure of activin A in complex with an ActRIIB-Alk4 fusion reveal insight into activin receptor interactions Deposited 2021-05-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 10 PDB declaration: decameric	Chain A 311–426（116 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；17.7 mg/ml complex in 20 mM HEPES, 200 mM NaCl pH 7.5. 100 + 100 nl sitting drop in a MRC 3-well plate with reservoir 0.1 M Na cacodylate pH 6.5 and 17 % (w/v) PEG 4000).	Resolution 3.27 Å R-free 0.269
7U5P CRYSTAL STRUCTURE OF THE ACTIVIN RECEPTOR TYPE-2A LIGAND BINDING DOMAIN IN COMPLEX WITH ACTIVIN-A Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 311–426（116 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；294 K；100mM Sodium Citrate, 17%PEG 3000	Resolution 3.14 Å R-free 0.276
7U5P CRYSTAL STRUCTURE OF THE ACTIVIN RECEPTOR TYPE-2A LIGAND BINDING DOMAIN IN COMPLEX WITH ACTIVIN-A Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 311–426（116 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；294 K；100mM Sodium Citrate, 17%PEG 3000	Resolution 3.14 Å R-free 0.276
7U5P CRYSTAL STRUCTURE OF THE ACTIVIN RECEPTOR TYPE-2A LIGAND BINDING DOMAIN IN COMPLEX WITH ACTIVIN-A Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 311–426（116 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；294 K；100mM Sodium Citrate, 17%PEG 3000	Resolution 3.14 Å R-free 0.276
7U5P CRYSTAL STRUCTURE OF THE ACTIVIN RECEPTOR TYPE-2A LIGAND BINDING DOMAIN IN COMPLEX WITH ACTIVIN-A Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 311–426（116 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；294 K；100mM Sodium Citrate, 17%PEG 3000	Resolution 3.14 Å R-free 0.276
9I5W Structure of mature Activin A from DMSO solvent optimisation of XChem fragment screen Deposited 2025-01-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 311–426（116 aa） Chain B 311–426（116 aa）	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

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

Follistatin

Homo sapiens

UniProt P19883

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 30–317 Chain D； UniProt 30–317	Fragment：Follistatin-288	Inhibin beta A chain × 2 （P08476） IR3 IRIDIUM (III) ION × 5 MLI MALONATE ION × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；PEG 3350, 200 mM Malonate, pH 7.0, vapor diffusion, hanging drop, temperature 295K	Resolution 2.80 Å R-free 0.297

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.

Other PDB	Difference from Current Entry 2B0U	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2P6A The structure of the Activin:Follistatin 315 complex Deposited 2007-03-16	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 30–344（315 aa） Chain D 30–344（315 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；20-23% PEG 1000, 200mM MgCl2, 3% EtOH, 20mM Trimethyl-amine HCl, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298 K	Resolution 3.40 Å R-free 0.324
3HH2 Crystal structure of the myostatin:follistatin 288 complex Deposited 2009-05-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 30–317（288 aa） Fragment：UNP residues 30-317 Chain D 30–317（288 aa） Fragment：UNP residues 30-317	Not recorded	PO4 PHOSPHATE ION × 3 CIT CITRIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；PEG 1000, Ethanol, Phosphate/citrate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.15 Å R-free 0.249
5JHW Crystal Structure of the GDF11:Follistatin 288 complex Deposited 2016-04-21	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 30–317（288 aa） Fragment：UNP residues 30-317 Chain D 30–317（288 aa） Fragment：UNP residues 30-317	Not recorded	PO4 PHOSPHATE ION × 3 FLC CITRATE ANION × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；298 K；100mM Phosphate/Citrate pH 4.2, 14% EtOH, 1% PEG 1000	Resolution 2.35 Å R-free 0.247

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FST_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–288； UniProt 30–317 Author chain D； PDBConstruct 1–288； UniProt 30–317

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2b0u
Deposition date deposition_date	2005-09-14
Structure title title	The Structure of the Follistatin:Activin Complex
Keywords keywords	activin, follistatin, TGF-beta, morphogen, inhibin, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	32.33 Å
Radius of gyration Rg (electron density) rg_electron	31.62 Å
Forward intensity I(0) i0	144786000.00
Molecular weight molecular_weight	86239.0 kDa
Excluded volume excluded_volume	103620 Å³
Envelope volume envelope_volume	150470 Å³
Hydration-shell volume shell_volume	39767 Å³
Envelope diameter envelope_diameter	112.6 Å
Shell Rg shell_rg	38.94 Å
Envelope Rg envelope_rg	30.75 Å
Shape Rg shape_rg	31.61 Å
Total Rg total_rg	32.26 Å
Total atoms total_atoms	5904
Residues n_residues	799
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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

Maximum dimension Dmax dmax	102.8 Å
Rg (real space) rg_real	32.25 Å
Rg uncertainty (real space) rg_real_error	0.64 Å
I(0) (real space) i0_real	1.4480e+08
I(0) uncertainty (real space) i0_real_error	2.1980e+06
Rg (reciprocal space) rg_reciprocal	32.28 Å
I(0) (reciprocal space) i0_reciprocal	144800000.0000
Solution quality estimate total_estimate	0.9039
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	37.8 Å
Skewness Skewness skewness	0.239
Kurtosis Kurtosis kurtosis	-0.456
Angular range angular_range	— – 0.2450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12410000.0000
Real-space data points n_real_points	50
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.916

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Inhibin beta A chain
Molecular weight formula_weight	12991.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	6045

GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Cricetulus griseus

Entity 2 Entity 2 polymer

Description description	Follistatin
Molecular weight formula_weight	31592.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

GNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGRCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCN

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Cricetulus griseus

Entity 3 Entity 3 non-polymer

Description description	IRIDIUM (III) ION
Molecular weight formula_weight	192.2 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 4 Entity 4 non-polymer

Description description	MALONATE ION
Molecular weight formula_weight	102.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 non-polymer

Description description	(4S)-2-METHYL-2,4-PENTANEDIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	141

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2b0ua_
Class class	g — Small proteins
Fold Fold fold	g.17 — Cystine-knot cytokines
Superfamily Superfamily superfamily	g.17.1 — Cystine-knot cytokines
Family Family family	g.17.1.2 — Transforming growth factor (TGF)-beta

Domain ID domain_id	d2b0ub_
Class class	g — Small proteins
Fold Fold fold	g.17 — Cystine-knot cytokines
Superfamily Superfamily superfamily	g.17.1 — Cystine-knot cytokines
Family Family family	g.17.1.2 — Transforming growth factor (TGF)-beta

CATH v4.4 (10 domains)

Domain ID domain_id	2b0uA00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily	10 — Cystine-knot cytokines

Domain ID domain_id	2b0uB00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily	10 — Cystine-knot cytokines

Domain ID domain_id	2b0uC01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	290 — Extracellular Matrix Fibrillin
Homologous superfamily homologous superfamily	10 — TGF-beta binding (TB) domain

Domain ID domain_id	2b0uC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	2b0uC03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	2b0uC04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	2b0uD01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	290 — Extracellular Matrix Fibrillin
Homologous superfamily homologous superfamily	10 — TGF-beta binding (TB) domain

Domain ID domain_id	2b0uD02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	2b0uD03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	2b0uD04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	30 —

▶

8. Citations (1)

▶

Unit-cell length a length_a	109.250 Å
Unit-cell length b length_b	120.820 Å
Unit-cell length c length_c	70.570 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	19.350 Å
R factor r_factor	0.3010
R_work r_work	0.2650
R_free r_free	0.2970

fit	/app/data/saxs_computation/b0/2b0u/2b0u.fit
pddf	/app/data/pr_computation/b0/2b0u/2b0u.pr.out
profile	/app/data/saxs_computation/b0/2b0u/2b0u.dat

The Structure of the Follistatin:Activin Complex

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

Inhibin beta A chain

State in the Current Structure

Other States of the Same Protein in the Database

Follistatin

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (2 domains)

CATH v4.4 (10 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)