SAXSdb — 4ak3

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

COLLAGEN ALPHA-1(III) 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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 1222–1466	Fragment：CPROPEPTIDE, RESIDUES 1222-1466 Mutation：YES	CA CALCIUM ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 3.50 Å R-free 0.337

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 4AK3	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 mutation/modification 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 ligand/ion 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
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 mutation/modification Different ligand/ion 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
7WWS Structure of a triple-helix region of human collagen type III from Trautec Deposited 2022-02-14	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 976–1002（27 aa） Chain B 976–1002（27 aa） Chain C 976–1002（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；0.2M MgAc2, 0.1M Na cacodylate pH6.5, 20% PEG 8000	Resolution 1.30 Å R-free 0.158
7XAN Structure of a triple-helix region of human collagen type III from Trautec Deposited 2022-03-18	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 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 12–256； UniProt 1222–1466

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	4ak3
Deposition date deposition_date	2012-02-21
Structure title title	Crystal structure of Human fibrillar procollagen type III C- propeptide trimer
Keywords keywords	STRUCTURAL PROTEIN, FIBRILLAR COLLAGEN, EXTACELLULAR MATRIX, FIBROSIS; 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	20.87 Å
Radius of gyration Rg (electron density) rg_electron	20.24 Å
Forward intensity I(0) i0	9989780.00
Molecular weight molecular_weight	22025.0 kDa
Excluded volume excluded_volume	26798 Å³
Envelope volume envelope_volume	33019 Å³
Hydration-shell volume shell_volume	15103 Å³
Envelope diameter envelope_diameter	85.5 Å
Shell Rg shell_rg	24.60 Å
Envelope Rg envelope_rg	20.83 Å
Shape Rg shape_rg	20.25 Å
Total Rg total_rg	20.86 Å
Total atoms total_atoms	1554
Residues n_residues	227
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	82.7 Å
Rg (real space) rg_real	21.14 Å
Rg uncertainty (real space) rg_real_error	0.84 Å
I(0) (real space) i0_real	9.9900e+06
I(0) uncertainty (real space) i0_real_error	1.4300e+05
Rg (reciprocal space) rg_reciprocal	21.09 Å
I(0) (reciprocal space) i0_reciprocal	9990000.0000
Solution quality estimate total_estimate	0.7351
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.4 Å
Skewness Skewness skewness	0.697
Kurtosis Kurtosis kurtosis	0.271
Angular range angular_range	— – 0.3800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1984000.0000
Real-space data points n_real_points	70
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.406; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.364; Smooth: 0.971

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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	COLLAGEN ALPHA-1(III) CHAIN
Molecular weight formula_weight	28815.3 kDa
Mutation mutation	YES
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	1555

ETGHHHHHHSADEPMDFKINTDEIMTSLKSVNGQIESLISPDGSRKNPARNCRDLKFCHPELKSGEYWVDPNQGCKLDAIKVFCNMETGETCISANPLNVPRKHWWTDSSAEKKHVWFGESMDGGFQFSYGNPELPEDVLDVQLAFLRLLSSRASQQITYHCKNSIAYMDQASGNVKKALKLMGSNEGEFKAEGNSKFTYTVLEDGCTKHTGEWSKTVFEYRTRKAVRLPIVDIAPYDIGGPDQEFGVDVGPVCFL

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 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 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	1

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	4ak3A00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	1000 —

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8. Citations (2)

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Unit-cell length a length_a	86.047 Å
Unit-cell length b length_b	86.047 Å
Unit-cell length c length_c	72.952 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	6

Space group space_group	P 3 2 1
Space-group number int_tables_number	150
Crystal system crystal_system	—

Resolution resolution	3.500 Å
Low-resolution limit resolution_low	43.020 Å
R factor r_factor	0.2854
R_work r_work	0.2828
R_free r_free	0.3372

fit	/app/data/saxs_computation/ak/4ak3/4ak3.fit
pddf	/app/data/pr_computation/ak/4ak3/4ak3.pr.out
profile	/app/data/saxs_computation/ak/4ak3/4ak3.dat

Crystal structure of Human fibrillar procollagen type III C- propeptide trimer

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