SAXSdb — 5hly

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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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 30–426	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

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 5HLY	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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 oligomeric state 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 mutation/modification 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
2B0U The Structure of the Follistatin:Activin Complex Deposited 2005-09-14	Different construct Different mutation/modification Different oligomeric state 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） Fragment：Activin (mature form) Chain B 311–426（116 aa） Fragment：Activin (mature form)	Not recorded	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
2P6A The structure of the Activin:Follistatin 315 complex Deposited 2007-03-16	Different construct Different mutation/modification 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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
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 mutation/modification 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 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 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 mutation/modification 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 11–383； UniProt 30–426

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	5hly
Deposition date deposition_date	2016-01-15
Structure title title	Structure of Pro-Activin A Precursor at 2.3 A Resolution
Keywords keywords	Growth factor, Precursor, Signalling, 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	29.58 Å
Radius of gyration Rg (electron density) rg_electron	29.30 Å
Forward intensity I(0) i0	21207900.00
Molecular weight molecular_weight	34322.0 kDa
Excluded volume excluded_volume	42435 Å³
Envelope volume envelope_volume	60956 Å³
Hydration-shell volume shell_volume	18154 Å³
Envelope diameter envelope_diameter	92.4 Å
Shell Rg shell_rg	34.83 Å
Envelope Rg envelope_rg	28.93 Å
Shape Rg shape_rg	29.34 Å
Total Rg total_rg	29.78 Å
Total atoms total_atoms	2373
Residues n_residues	291
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	92.4 Å
Rg (real space) rg_real	29.74 Å
Rg uncertainty (real space) rg_real_error	0.74 Å
I(0) (real space) i0_real	2.1210e+07
I(0) uncertainty (real space) i0_real_error	3.0690e+05
Rg (reciprocal space) rg_reciprocal	29.68 Å
I(0) (reciprocal space) i0_reciprocal	21210000.0000
Solution quality estimate total_estimate	0.8498
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	22.2 Å
Skewness Skewness skewness	0.271
Kurtosis Kurtosis kurtosis	-0.933
Angular range angular_range	— – 0.2700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1545000.0000
Real-space data points n_real_points	55
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.829; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.662; Smooth: 0.894

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Inhibin beta A chain
Molecular weight formula_weight	43664.0 kDa
Mutation mutation	C35S, C38S, deletion:K259-D282
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2406

MSHHHHHHSMSAAPDSPSSALAALPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS

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	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	25

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8. Citations (1)

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Unit-cell length a length_a	46.561 Å
Unit-cell length b length_b	46.561 Å
Unit-cell length c length_c	444.921 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 61 2 2
Space-group number int_tables_number	178
Crystal system crystal_system	—

Resolution resolution	2.302 Å
Low-resolution limit resolution_low	74.150 Å
R factor r_factor	0.2049
R_work r_work	0.2025
R_free r_free	0.2524

fit	/app/data/saxs_computation/hl/5hly/5hly.fit
pddf	/app/data/pr_computation/hl/5hly/5hly.pr.out
profile	/app/data/saxs_computation/hl/5hly/5hly.dat

Structure of Pro-Activin A Precursor at 2.3 A Resolution

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

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