SAXSdb — 7wws

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

Collagen alpha-1(III) chain

OrganismNot specified

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 976–1002 Chain B； UniProt 976–1002 Chain C； UniProt 976–1002	Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；0.2M MgAc2, 0.1M Na cacodylate pH6.5, 20% PEG 8000	Resolution 1.30 Å R-free 0.158

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 7WWS	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2V53 Crystal structure of a SPARC-collagen complex Deposited 2008-10-01	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 564–584（21 aa） Fragment：RESIDUES 564-584 Chain C 564–584（21 aa） Fragment：RESIDUES 564-584 Chain D 564–584（21 aa） Fragment：RESIDUES 564-584	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；pH 5.5	Resolution 3.20 Å R-free 0.320
3DMW Crystal structure of human type III collagen G982-G1023 containing C-terminal cystine knot Deposited 2008-07-01	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1158–1199（42 aa） Fragment：UNP residues 1158-1199 Chain B 1158–1199（42 aa） Fragment：UNP residues 1158-1199 Chain C 1158–1199（42 aa） Fragment：UNP residues 1158-1199	Mutation：Q1183M Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q1183M Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q1183M Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；30% PEG 550, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.30 Å R-free 0.274
4AE2 Crystal structure of Human fibrillar procollagen type III C- propeptide trimer Deposited 2012-01-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1222–1466（245 aa） Fragment：CPROPEPTIDE OF PROCOLLAGEN III, RESIDUES 1222-1466 Chain B 1222–1466（245 aa） Fragment：CPROPEPTIDE OF PROCOLLAGEN III, RESIDUES 1222-1466 Chain C 1222–1466（245 aa） Fragment：CPROPEPTIDE OF PROCOLLAGEN III, RESIDUES 1222-1466	Mutation：YES Mutation：YES Mutation：YES	CA CALCIUM ION × 3 NO3 NITRATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；20% PEG 3350, 0.1 M BIS TRIS PROPANE PH 6.5, POTASSIUM NITRATE 0.2 M	Resolution 1.68 Å R-free 0.214
4AEJ Crystal structure of Human fibrillar procollagen type III C- propeptide trimer Deposited 2012-01-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1222–1466（245 aa） Fragment：CPROPEPTIDE OF PROCOLLAGEN III, RESIDUES 1222-1466 Chain B 1222–1466（245 aa） Fragment：CPROPEPTIDE OF PROCOLLAGEN III, RESIDUES 1222-1466 Chain C 1222–1466（245 aa） Fragment：CPROPEPTIDE OF PROCOLLAGEN III, RESIDUES 1222-1466	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 3 GOL GLYCEROL × 7	X-RAY DIFFRACTION X-ray crystallization conditions 20% PEG 3350, 0.2 M NACL	Resolution 2.21 Å R-free 0.237
4AK3 Crystal structure of Human fibrillar procollagen type III C- propeptide trimer Deposited 2012-02-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1222–1466（245 aa） Fragment：CPROPEPTIDE, RESIDUES 1222-1466	Mutation：YES	CA CALCIUM ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.50 Å R-free 0.337
6FZV Crystal structure of the metalloproteinase enhancer PCPE-1 bound to the procollagen C propeptide trimer (short) Deposited 2018-03-15	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 1222–1466（245 aa） Chain B 1222–1466（245 aa） Chain C 1222–1466（245 aa）	Not recorded	CA CALCIUM ION × 5 FLC CITRATE ANION × 3 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；20 mg/ml protein in 20 mM HEPES pH 7.5, 180 mM NaCl, 2.5 mM calcium chloride; 0.2 M potassium citrate, 16% PEG3350	Resolution 2.70 Å R-free 0.258
6FZW Crystal structure of the metalloproteinase enhancer PCPE-1 bound to the procollagen C propeptide trimer (long) Deposited 2018-03-15	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 1185–1466（282 aa） Chain B 1185–1466（282 aa） Chain C 1185–1466（282 aa）	Not recorded	CA CALCIUM ION × 5 FLC CITRATE ANION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；20 mg/ml protein in 20 mM HEPES pH 7.5, 180 mM NaCl, 2.5 mM calcium chloride; 0.2 M ammonium citrate, 18% PEG3350	Resolution 2.78 Å R-free 0.271
7WWR Structure of a triple-helix region of human collagen type III from Trautec Deposited 2022-02-14	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 973–1002（30 aa） Chain B 973–1002（30 aa） Chain C 973–1002（30 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M MIB pH5.0, 25% PEG 1500	Resolution 1.30 Å R-free 0.194
7XAN Structure of a triple-helix region of human collagen type III from Trautec Deposited 2022-03-18	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 922–948（27 aa） Chain B 922–948（27 aa） Chain C 922–948（27 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.04M K phosphate monobasic, 16% w/v PEG 8000, 20% v/v Glycerol	Resolution 1.50 Å R-free 0.200

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CO3A1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–27； UniProt 976–1002 Author chain B； PDBConstruct 1–27； UniProt 976–1002 Author chain C； PDBConstruct 1–27； UniProt 976–1002

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	7wws
Deposition date deposition_date	2022-02-14
Structure title title	Structure of a triple-helix region of human collagen type III from Trautec
Keywords keywords	Human collagen type III Triple-helix region Crystal structure Integrin recognition motif, STRUCTURAL PROTEIN; STRUCTURAL 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	21.40 Å
Radius of gyration Rg (electron density) rg_electron	23.01 Å
Forward intensity I(0) i0	1326190.00
Molecular weight molecular_weight	7409.0 kDa
Excluded volume excluded_volume	8986 Å³
Envelope volume envelope_volume	11659 Å³
Hydration-shell volume shell_volume	6149 Å³
Envelope diameter envelope_diameter	86.5 Å
Shell Rg shell_rg	22.68 Å
Envelope Rg envelope_rg	23.59 Å
Shape Rg shape_rg	22.99 Å
Total Rg total_rg	23.01 Å
Total atoms total_atoms	522
Residues n_residues	63
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	56.4 Å
Rg (real space) rg_real	19.30 Å
Rg uncertainty (real space) rg_real_error	0.18 Å
I(0) (real space) i0_real	1.2560e+06
I(0) uncertainty (real space) i0_real_error	1.3210e+04
Rg (reciprocal space) rg_reciprocal	22.10 Å
I(0) (reciprocal space) i0_reciprocal	1326000.0000
Solution quality estimate total_estimate	0.5475
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	0
Primary peak position r_peak_primary	— Å
Skewness Skewness skewness	0.399
Kurtosis Kurtosis kurtosis	-0.879
Angular range angular_range	— – 0.3700 Å⁻¹
Current regularization parameter α current_alpha	1.8450
Highest regularization parameter α highest_alpha	23670.0000
Real-space data points n_real_points	69
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.001; Oscil: 0.705; Stabil: 0.975; Sysdev: 0.000; Positv: 1.000; Valcen: 0.123; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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Unit-cell length a length_a	18.582 Å
Unit-cell length b length_b	19.320 Å
Unit-cell length c length_c	74.234 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	96.89 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.300 Å
Low-resolution limit resolution_low	24.578 Å
R factor r_factor	—
R_work r_work	0.1144
R_free r_free	0.1582

Description description	Collagen alpha-1(III) chain
Molecular weight formula_weight	2464.6 kDa
Source method src_method	syn
Copy count entity_count	3

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	681

Structure of a triple-helix region of human collagen type III from Trautec

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

Collagen alpha-1(III) 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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	156

fit	/app/data/saxs_computation/ww/7wws/7wws.fit
pddf	/app/data/pr_computation/ww/7wws/7wws.pr.out
profile	/app/data/saxs_computation/ww/7wws/7wws.dat