SAXSdb — 8udz

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

Transforming growth factor beta-1 proprotein

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	Other combination Heteromer Protein × 6 其他Polymer 1 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 30–390 Chain B； UniProt 30–390	Mutation：C33S, R278A	LTBP-49247 Fab Heavy Chain × 2 LTBP-49247 Fab Light Chain × 2 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；15% PEG 3350, 12% Tacsimate (pH 4.0), 10 mM Magnesium Chloride	Resolution 2.21 Å R-free 0.264

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 8UDZ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1KLA SOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 1-17 OF 33 STRUCTURES Deposited 1996-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 279–390（112 aa） Chain B 279–390（112 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.2	Resolution not provided
1KLC SOLUTION STRUCTURE OF TGF-B1, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1996-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 279–390（112 aa） Chain B 279–390（112 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.2	Resolution not provided
1KLD SOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 18-33 OF 33 STRUCTURES Deposited 1996-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 279–390（112 aa） Chain B 279–390（112 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.2	Resolution not provided
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 A 279–390（112 aa） Chain B 279–390（112 aa）	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 C 279–390（112 aa） Chain D 279–390（112 aa）	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 A 279–390（112 aa） Chain B 279–390（112 aa） Chain C 279–390（112 aa） Chain D 279–390（112 aa）	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
4KV5 scFv GC1009 in complex with TGF-beta1. Deposited 2013-05-22	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 C 279–390（112 aa） Fragment：unp residues 279-390 Chain D 279–390（112 aa） Fragment：unp residues 279-390	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5；294 K；16% PEG 4K, 0.1 M citrate, 4% 2-propanol , pH 5.0, VAPOR DIFFUSION, temperature 294K	Resolution 3.00 Å R-free 0.300
4KV5 scFv GC1009 in complex with TGF-beta1. Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 279–390（112 aa） Fragment：unp residues 279-390 Chain B 279–390（112 aa） Fragment：unp residues 279-390	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5；294 K；16% PEG 4K, 0.1 M citrate, 4% 2-propanol , pH 5.0, VAPOR DIFFUSION, temperature 294K	Resolution 3.00 Å R-free 0.300
5FFO Integrin alpha V beta 6 in complex with pro-TGF-beta Deposited 2015-12-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain C 34–390（357 aa） Fragment：UNP residues 34-390 Chain D 34–390（357 aa） Fragment：UNP residues 34-390 Chain G 34–390（357 aa） Fragment：UNP residues 34-390 Chain H 34–390（357 aa） Fragment：UNP residues 34-390	Not recorded	CA CALCIUM ION × 8 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 MN MANGANESE (II) ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；8% PEG8000 0.1M Immidazole	Resolution 3.49 Å R-free 0.277
5VQP Crystal structure of human pro-TGF-beta1 Deposited 2017-05-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 30–390（361 aa）	Mutation：C4S,N107Q,N147Q	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.3；289 K；100 mM MES pH6.3, 1.68 M Ammonium Sulfate, 11% Dioxane	Resolution 2.90 Å R-free 0.293
6GFF Structure of GARP (LRRC32) in complex with latent TGF-beta1 and MHG-8 Fab Deposited 2018-04-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 30–278（249 aa） Fragment：LAP Chain B 279–390（112 aa） Fragment：Mature Chain C 30–278（249 aa） Fragment：LAP Chain D 279–390（112 aa） Fragment：Mature	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；15% (w/v) PEG4000, 0.1 M HEPES pH 6.75	Resolution 3.10 Å R-free 0.268
6GFF Structure of GARP (LRRC32) in complex with latent TGF-beta1 and MHG-8 Fab Deposited 2018-04-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 7 PDB declaration: heptameric	Chain E 30–278（249 aa） Fragment：LAP Chain F 279–390（112 aa） Fragment：Mature Chain G 30–278（249 aa） Fragment：LAP Chain H 279–390（112 aa） Fragment：Mature	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；15% (w/v) PEG4000, 0.1 M HEPES pH 6.75	Resolution 3.10 Å R-free 0.268
6P7J Crystal structure of Latency Associated Peptide unbound to TGF-beta1 Deposited 2019-06-05	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 30–278（249 aa）	Mutation：R249A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions BATCH MODE；pH 4.6；293 K；Reservoir composition: 20% PEG3350, 300 mM NaAc pH 4.6	Resolution 3.50 Å R-free 0.322
7Y1R Human L-TGF-beta1 in complex with the anchor protein LRRC33 Deposited 2022-06-08	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 30–390（361 aa） Chain B 30–390（361 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.01 Å
7Y1T Complex of integrin alphaV/beta8 and L-TGF-beta1 at a ratio of 1:2 Deposited 2022-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 30–390（361 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CA CALCIUM ION × 5 MN MANGANESE (II) ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å
8C7H Cryo-EM Map of the latTGF-beta LHG-10 Fab complex Deposited 2023-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 30–278（249 aa） Fragment：LAP Chain B 279–390（112 aa） Fragment：Mature Chain C 30–278（249 aa） Fragment：LAP Chain D 279–390（112 aa） Fragment：Mature	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
8REW CryoEM structure of human GARP-lTGFbeta1 in complex with a Fab fragment derived from an activating antibody. Deposited 2023-12-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 1–390（390 aa） Fragment：LAP Chain B 1–390（390 aa） Fragment：LAP Chain C 1–390（390 aa） Fragment：LAP Chain D 1–390（390 aa） Fragment：LAP	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.98 Å
8VSC L-TGF-b1/GARP Deposited 2024-01-23	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 × 3 PDB declaration: trimeric	Chain A 1–390（390 aa） Chain B 1–390（390 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
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 A 279–390（112 aa） Fragment：Mature Chain B 279–390（112 aa） Fragment：Mature	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
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 A 279–390（112 aa） Fragment：Mature Chain B 279–390（112 aa） Fragment：Mature	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
9VJJ Crystal Structure of human Latent TGF-beta1 in complex with SOF10 Deposited 2025-06-20	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 30–390（361 aa） Chain B 30–390（361 aa）	Mutation：C33S Mutation：C33S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.2M Sodium acetate trihydrate, 0.1M Imidazole hydrochloride (pH 8.0), 10.0% w/v Polyethylene glycol 8000	Resolution 2.48 Å R-free 0.310

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

View Construct and Data Evidence

UniProt name	TGFB1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–361； UniProt 30–390 Author chain B； PDBConstruct 1–361； UniProt 30–390

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	8udz
Deposition date deposition_date	2023-09-29
Structure title title	The Structure of LTBP-49247 Fab Bound to TGFbeta1 Small Latent Complex
Keywords keywords	Growth factor, antibody, fibrosis, TGFbeta, SIGNALING PROTEIN, SIGNALING PROTEIN-IMMUNE SYSTEM complex; SIGNALING PROTEIN/IMMUNE SYSTEM
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	49.70 Å
Radius of gyration Rg (electron density) rg_electron	50.06 Å
Forward intensity I(0) i0	369963000.00
Molecular weight molecular_weight	157710.0 kDa
Excluded volume excluded_volume	196960 Å³
Envelope volume envelope_volume	296330 Å³
Hydration-shell volume shell_volume	52058 Å³
Envelope diameter envelope_diameter	170.4 Å
Shell Rg shell_rg	49.64 Å
Envelope Rg envelope_rg	49.60 Å
Shape Rg shape_rg	50.07 Å
Total Rg total_rg	50.02 Å
Total atoms total_atoms	11092
Residues n_residues	1422
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	170.4 Å
Rg (real space) rg_real	50.01 Å
Rg uncertainty (real space) rg_real_error	1.98 Å
I(0) (real space) i0_real	3.7000e+08
I(0) uncertainty (real space) i0_real_error	7.4150e+06
Rg (reciprocal space) rg_reciprocal	49.70 Å
I(0) (reciprocal space) i0_reciprocal	369800000.0000
Solution quality estimate total_estimate	0.8566
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	42.6 Å
Skewness Skewness skewness	0.299
Kurtosis Kurtosis kurtosis	-0.709
Angular range angular_range	— – 0.1600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	22120000.0000
Real-space data points n_real_points	33
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.850; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.824; Smooth: 0.756

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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	Transforming growth factor beta-1 proprotein
Molecular weight formula_weight	41221.0 kDa
Mutation mutation	C33S, R278A
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	11329

LSTSKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRAALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS

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	Homo sapiens

Entity 2 Entity 2 polymer

Description description	LTBP-49247 Fab Heavy Chain
Molecular weight formula_weight	25100.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

QVQLVESGGGVVQPGRSLRLSCAASGFTFRSYVMHWVRQAPGKGLEWVAVISHEGSLKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARPRIAARRGGFGYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHHHHHH

来源 Source

来源生物 organism	Homo sapiens
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	LTBP-49247 Fab Light Chain
Molecular weight formula_weight	23484.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

NFMLTQPHSVSESPGKTVTISCTRSSGNIDNNYVQWYQQRPGSSPTTVIYEDNQRPSGVPDRFSGSIDSSSNSASLTISGLKTEDEADYYCQSYDYDTQGVVFGGGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS

来源 Source

来源生物 organism	Homo sapiens
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 4 Entity 4 branched

Description description	;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	910.8 kDa
Source method src_method	man
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	2

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	232

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8. Citations (1)

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Unit-cell length a length_a	73.495 Å
Unit-cell length b length_b	141.905 Å
Unit-cell length c length_c	186.122 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 2 21 21
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.210 Å
Low-resolution limit resolution_low	73.500 Å
R factor r_factor	0.2333
R_work r_work	0.2316
R_free r_free	0.2643

fit	/app/data/saxs_computation/ud/8udz/8udz.fit
pddf	/app/data/pr_computation/ud/8udz/8udz.pr.out
profile	/app/data/saxs_computation/ud/8udz/8udz.dat

The Structure of LTBP-49247 Fab Bound to TGFbeta1 Small Latent Complex

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

Transforming growth factor beta-1 proprotein

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 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 branched

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)