SAXSdb — 8g4k

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

TGF-beta receptor type-2

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 46–155	Fragment：ECD (UNP residues 46-155)	5HCS_TGFBR2_1 × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.4；300 K；20% PEG5000 MME, 0.2-0.4 M ammonium sulfate, 0.1 M Tris, pH 7.4, 16-32% glycerol	Resolution 1.24 Å R-free 0.196

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 8G4K	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1KTZ Crystal Structure of the Human TGF-beta Type II Receptor Extracellular Domain in Complex with TGF-beta3 Deposited 2002-01-18	Different construct 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 38–159（122 aa） Fragment：Extracellular Domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions HANGING DROP VAPOR DIFFUSION USING A WELL SOLUTION CONTAINING 20% (V/V) 2-METHYL-2,4-PENTANEDIOL AND 0.1 M CITRATE PH 4.0	Resolution 2.15 Å R-free 0.215
1M9Z CRYSTAL STRUCTURE OF HUMAN TGF-BETA TYPE II RECEPTOR LIGAND BINDING DOMAIN Deposited 2002-07-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 49–159（111 aa） Fragment：Extracellular	Mutation：Q26A,K97T	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；PEG 2000, sodium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.05 Å R-free 0.166
1PLO TRANSFORMING GROWTH FACTOR-BETA TYPE II RECEPTOR EXTRACELLULAR DOMAIN Deposited 2003-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 38–159（122 aa）	Mutation：N19A	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；300 K；Ionic strength (raw mmCIF value) 25mM sodium acetate, 25mM NaCl, pH 5.5；Pressure ambient NMR measurement conditions pH 5.1；300 K；Ionic strength (raw mmCIF value) 25mM sodium acetate, 25mM NaCl；Pressure ambient NMR measurement conditions pH 5.5；313 K；Ionic strength (raw mmCIF value) 25mM sodium acetate, 25mM NaCl；Pressure ambient NMR sample composition 1mM ecTbR2 U-15N, 25mM sodium acetate, 25mM NaCl, 95% H2O, 5% D2O \| 95% H2O/5% D2O NMR sample composition 1mM ecTbR2 U-15N, 13C, 25mM sodium acetate, 25mM NaCl, 95% H2O, 5% D2O \| 95% H2O/5% D2O NMR sample composition 1mM ecTbR2 U-15N, 13C, 25mM sodium acetate, 25mM NaCl, 99.99% D2O \| 99.99% D2O NMR sample composition 1mM ecTbR2 U-15N, 25mM sodium acetate, 25mM NaCl, 4% (w/v) 1,2-di-O-hexyl-sn-glycero-3-phosphocholine (6-O-PC) and 1,2-di-O-tetradecyl-sn-glycero-3-phosphocholine (14-O-PC) mixed in a molar ratio of 1:3, 95% H2O, 5% D2O \| 95% H2O/5% D2O NMR sample composition 1mM ecTbR2 U-15N, 13C, 25mM sodium acetate, 25mM NaCl, 4% (w/v) 1,2-di-O-hexyl-sn-glycero-3-phosphocholine (6-O-PC) and 1,2-di-O-tetradecyl-sn-glycero-3-phosphocholine (14-O-PC) mixed in a molar ratio of 1:3, 95% H2O, 5% D2O \| 95% H2O/5% D2O	Resolution not provided
2PJY Structural basis for cooperative assembly of the TGF-beta signaling complex Deposited 2007-04-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 42–149（108 aa） Fragment：extracellular domain	Mutation：N42A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；10-20% PEG 3350, 0.4-0.65 M calcium acetate, 0.1-0.25M NaCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.00 Å R-free 0.297
3KFD Ternary complex of TGF-b1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily Deposited 2009-10-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain E 38–153（116 aa） Fragment：extracellular domain Chain F 38–153（116 aa） Fragment：extracellular domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；298 K；8-15% Peg 4000-8000, pH 7.0, VAPOR DIFFUSION, temperature 298K	Resolution 3.00 Å R-free 0.268
3KFD Ternary complex of TGF-b1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily Deposited 2009-10-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain G 38–153（116 aa） Fragment：extracellular domain Chain H 38–153（116 aa） Fragment：extracellular domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；298 K；8-15% Peg 4000-8000, pH 7.0, VAPOR DIFFUSION, temperature 298K	Resolution 3.00 Å R-free 0.268
3KFD Ternary complex of TGF-b1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily Deposited 2009-10-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain E 38–153（116 aa） Fragment：extracellular domain Chain F 38–153（116 aa） Fragment：extracellular domain Chain G 38–153（116 aa） Fragment：extracellular domain Chain H 38–153（116 aa） Fragment：extracellular domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；298 K；8-15% Peg 4000-8000, pH 7.0, VAPOR DIFFUSION, temperature 298K	Resolution 3.00 Å R-free 0.268
4P7U Extracellular domain of type II Transforming Growth Factor Beta receptor in complex with NDSB-201 Deposited 2014-03-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 75–184（110 aa） Fragment：extracellular domain, UNP residues 74-175	Mutation：Q26A K97T	1PS 3-PYRIDINIUM-1-YLPROPANE-1-SULFONATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；100 mM sodium citrate, 30% PEG 2000	Resolution 1.50 Å R-free 0.206
4XJJ Extracellular domain of type II Transforming Growth Factor Beta receptor in complex with 2-(2-Hydroxyethyl)NDSB-201 Deposited 2015-01-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 50–159（110 aa） Fragment：ligand binding domain (UNP reisudes 50-159)	Mutation：K97T	41D 3-[2-(2-hydroxyethyl)pyridinium-1-yl]propane-1-sulfonate × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；100 mM sodium citrate, 30% PEG 2000	Resolution 1.40 Å R-free 0.185
5E8V TGF-BETA RECEPTOR TYPE 2 KINASE DOMAIN (E431A,R433A,E485A,K488A,R493A,R495A) Deposited 2015-10-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 237–549（313 aa） Fragment：KINASE DOMAIN, UNP RESIDUES 237-549	Mutation：E431A,R433A,E485A,K488A,R493A,R495A	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；100 mm TRIS-HCl, PH 8.5, 150 mm MgCl2, 24%(w/v) PEG4000, 20%(v/v) glcyerol	Resolution 1.69 Å R-free 0.219
5E8Y TGF-BETA RECEPTOR TYPE 2 KINASE DOMAIN (E431A,R433A,E485A,K488A,R493A,R495A) IN COMPLEX WITH STAUROSPORINE Deposited 2015-10-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 237–549（313 aa） Fragment：KINASE DOMAIN, UNP RESIDUES 237-549	Mutation：E431A,R433A,E485A,K488A,R493A,R495A	STU STAUROSPORINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；100 mm TRIS-HCl, PH 8.5, 150 mm MgCl2, 24%(w/v) PEG4000, 20%(v/v) glcyerol	Resolution 2.05 Å R-free 0.227
5E91 TGF-BETA RECEPTOR TYPE 2 KINASE DOMAIN (E431A,R433A,E485A,K488A,R493A,R495A) IN COMPLEX WITH 3-AMINO-6-[4-(2- HYDROXYETHYL)PHENYL]-N-[4-(MORPHOLIN-4-YL)PYRIDIN-3-YL] PYRAZINE-2-CARBOXAMIDE Deposited 2015-10-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 237–549（313 aa） Fragment：KINASE DOMAIN, UNP RESIDUES 237-549	Mutation：E431A,R433A,E485A,K488A,R493A,R495A	5L4 3-amino-6-[4-(2-hydroxyethyl)phenyl]-N-[4-(morpholin-4-yl)pyridin-3-yl]pyrazine-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；100 mm TRIS-HCl, PH 8.5, 150 mm MgCl2, 24%(w/v) PEG4000, 20%(v/v) glcyerol	Resolution 2.42 Å R-free 0.242
5E92 TGF-BETA RECEPTOR TYPE 2 KINASE DOMAIN (E431A,R433A,E485A,K488A,R493A,R495A) IN COMPLEX WITH AMPPNP Deposited 2015-10-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 237–549（313 aa） Fragment：KINASE DOMAIN, UNP RESIDUES 237-549	Mutation：E431A,R433A,E485A,K488A,R493A,R495A	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；100 mm TRIS-HCl, PH 8.5, 150 mm MgCl2, 24%(w/v) PEG4000, 20%(v/v) glcyerol	Resolution 2.08 Å R-free 0.231
5QIN TGF-BETA RECEPTOR TYPE 2 KINASE DOMAIN IN COMPLEX WITH N- {4-[3-(6-METHOXYPYRIDIN-3-YL)-1H-PYRROLO[3,2-B]PYRIDIN-2- YL]PYRIDIN-2-YL}ACETAMIDE Deposited 2018-08-05	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 237–549（313 aa） Fragment：KINASE DOMAIN, UNP RESIDUES 237-549	Not recorded	J2V N-{4-[3-(6-methoxypyridin-3-yl)-1H-pyrrolo[3,2-b]pyridin-2-yl]pyridin-2-yl}acetamide × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；23%(w/v) PEG3350, 3%(v/v) glcyerol	Resolution 1.57 Å R-free 0.203
5TX4 Derivative of mouse TGF-beta2, with a deletion of residues 52-71 and K25R, R26K, L51R, A74K, C77S, L89V, I92V, K94R T95K, I98V single amino acid substitutions, bound to human TGF-beta type II receptor ectodomain residues 15-130 Deposited 2016-11-15	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 38–153（116 aa） Fragment：UNP residues 38-153	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.1 M Hepes, pH 7.5, 60 % v/v (+/-)-2-Methyl-2,4-pentanediol	Resolution 1.88 Å R-free 0.222
5TY4 MicroED structure of a complex between monomeric TGF-b and its receptor, TbRII, at 2.9 A resolution Deposited 2016-11-18	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 72–174（103 aa）	Not recorded	No recorded non-water small molecule	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.5 ul 20 mg/mL protein + 0.25 ul mother liquor + 0.2 ul seed stock in 100 mM HEPES/NaOH pH 7.5, 45% MPD	Resolution 2.90 Å R-free 0.328
7DV6 Discovery of Functionally Selective Transforming Growth Factor beta Type II Receptor (TGF-beta RII) Inhibitors as Anti-Fibrosis Agents Deposited 2021-01-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 237–549（313 aa）	Mutation：E431A,R433A,E485A,K488A,R493A,R495A	HJF 5-[(3S)-5,5-dimethyloxolan-3-yl]-6-methoxy-3-(2-methoxypyridin-4-yl)pyrazolo[1,5-a]pyrimidine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；12-22% PEG4000,3% Ethylene Glycol,16% glycerol, 160 mM MgCl2, 80 mM TrisHCl at pH 7.5-9.3,The 9.2 mg/mL of TGFbetaRII protein was incubated with 1mM compound at 277K for 1-2 hr	Resolution 2.39 Å R-free 0.224
8YGZ The Crystal Structure of TGF beta R2 kinase domain from Biortus. Deposited 2024-02-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 237–549（313 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	EDO 1,2-ETHANEDIOL × 10 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2M Li2SO4, 0.1M Tris-HCl pH8.5, 30% PEG4,000	Resolution 2.10 Å R-free 0.254
9B9F Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular domains of TGFBRI and TGFBRII Deposited 2024-04-02	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 D 42–153（112 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；0.2 M lithium sulfate, 0.1 M tris pH 8.5, 30 %(w/v) polyethylene glycol 4000	Resolution 3.00 Å R-free 0.278
9B9F Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular domains of TGFBRI and TGFBRII Deposited 2024-04-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain I 42–153（112 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；0.2 M lithium sulfate, 0.1 M tris pH 8.5, 30 %(w/v) polyethylene glycol 4000	Resolution 3.00 Å R-free 0.278
9E9G Heligmosomoides polygyrus TGF-beta Mimic 6 Domain 3 (TGM6-D3) Bound to Human TGF-beta Type II Receptor Extracellular Domain Deposited 2024-11-08	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 38–154（117 aa） Fragment：UNP residues 38-154	Not recorded	GOL GLYCEROL × 8 CL CHLORIDE ION × 2 NA SODIUM ION × 5 CAC CACODYLATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1 M sodium cacodylate, 25% w/v PEG4000, pH 6.5	Resolution 1.40 Å R-free 0.182
9FDY Betaglycan Orphan Domain (ratBGo) in complex with TGF-b1 and extracellular domain of TGFBRII Deposited 2024-05-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain D 42–153（112 aa） Chain E 42–153（112 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9FK5 Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular domains of TGFBRI and TGFBRII Deposited 2024-06-02	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain D 42–153（112 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.10 Å
9FKP Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-b1 and extracellular domain of TGFBRII Deposited 2024-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain D 42–153（112 aa） Chain E 42–153（112 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.72 Å

21 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TGFR2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 2–111； UniProt 46–155

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	8g4k
Deposition date deposition_date	2023-02-09
Structure title title	Complex of TbRII mini protein binder bound to the TbRII ECD
Keywords keywords	TbRII, TGF-b type II receptor, Computationally designed mini protein binder, MPB, 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	18.73 Å
Radius of gyration Rg (electron density) rg_electron	17.86 Å
Forward intensity I(0) i0	10648100.00
Molecular weight molecular_weight	24088.0 kDa
Excluded volume excluded_volume	30152 Å³
Envelope volume envelope_volume	35463 Å³
Hydration-shell volume shell_volume	16813 Å³
Envelope diameter envelope_diameter	63.1 Å
Shell Rg shell_rg	23.85 Å
Envelope Rg envelope_rg	18.28 Å
Shape Rg shape_rg	17.91 Å
Total Rg total_rg	18.67 Å
Total atoms total_atoms	3366
Residues n_residues	212
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	65.8 Å
Rg (real space) rg_real	18.70 Å
Rg uncertainty (real space) rg_real_error	0.55 Å
I(0) (real space) i0_real	1.0650e+07
I(0) uncertainty (real space) i0_real_error	1.5920e+05
Rg (reciprocal space) rg_reciprocal	18.71 Å
I(0) (reciprocal space) i0_reciprocal	10650000.0000
Solution quality estimate total_estimate	0.7796
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	22.5 Å
Skewness Skewness skewness	0.323
Kurtosis Kurtosis kurtosis	-0.315
Angular range angular_range	— – 0.4250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3057000.0000
Real-space data points n_real_points	74
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.725; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	5HCS_TGFBR2_1
Molecular weight formula_weight	11463.4 kDa
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	3721

SGSGLKELLKELNKAIASGDTETVRRILEELLELLKEAFEKGDYDLAISIASMAVKAASYIGDTETLKELLEILKKIKEKLKKEGDEAALKAVERNIKVVEKVA

来源 Source

来源生物 organism	synthetic construct
NCBI Class编号 ncbi_taxonomy_id	32630
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	TGF-beta receptor type-2
Molecular weight formula_weight	12800.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MKFPQLCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPKCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEYNT

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 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	201

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8. Citations (1)

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Unit-cell length a length_a	47.983 Å
Unit-cell length b length_b	57.175 Å
Unit-cell length c length_c	78.798 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.240 Å
Low-resolution limit resolution_low	46.280 Å
R factor r_factor	—
R_work r_work	0.1813
R_free r_free	0.1958

fit	/app/data/saxs_computation/g4/8g4k/8g4k.fit
pddf	/app/data/pr_computation/g4/8g4k/8g4k.pr.out
profile	/app/data/saxs_computation/g4/8g4k/8g4k.dat

Complex of TbRII mini protein binder bound to the TbRII ECD

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

TGF-beta receptor type-2

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 (4)

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 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)