SAXSdb — 5cva

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

Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 3	Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain × 1 （P02452,Q14055） Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain × 1 （P02452,Q14050） GLYCEROL × 1 water × 3	Consistent with protein count
2	Insufficient information	Heteromer	Protein 3	Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain × 1 （P02452,Q14055） Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain × 1 （P02452,Q14050） GLYCEROL × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CO1A2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 15–26； UniProt 484–495 Author chain D； PDBConstruct 15–26； UniProt 484–495

Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain

Homo sapiens

UniProt P20849

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 3	Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain × 1 （P02452,Q14055） Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain × 1 （P02452,Q14050） GLYCEROL × 1 water × 3	Consistent with protein count
2	Insufficient information	Heteromer	Protein 3	Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain × 1 （P02452,Q14055） Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain × 1 （P02452,Q14050） GLYCEROL × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CO9A1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 36–71； UniProt 754–789 Author chain D； PDBConstruct 36–71； UniProt 754–789

Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain

Homo sapiens

UniProt P02452

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 3	Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain × 1 （P08123,P20849） GLYCEROL × 1 water × 3	Consistent with protein count
2	Insufficient information	Heteromer	Protein 3	Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain × 1 （P08123,P20849） GLYCEROL × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CO1A1_HUMAN
Isoform	—
PDB entities	2, 3
Chains and sequence ranges	Author chain B； PDBConstruct 15–26； UniProt 572–583 Author chain E； PDBConstruct 15–26； UniProt 572–583 Author chain C； PDBConstruct 15–26； UniProt 572–583 Author chain F； PDBConstruct 15–26； UniProt 572–583

Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain

Homo sapiens

UniProt Q14055

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 3	Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain × 1 （P08123,P20849） Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain × 1 （P02452,Q14050） GLYCEROL × 1 water × 3	Consistent with protein count
2	Insufficient information	Heteromer	Protein 3	Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain × 1 （P08123,P20849） Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain × 1 （P02452,Q14050） GLYCEROL × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CO9A2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 36–71； UniProt 517–552 Author chain E； PDBConstruct 36–71； UniProt 517–552

Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain

Homo sapiens

UniProt Q14050

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 3	Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain × 1 （P08123,P20849） Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain × 1 （P02452,Q14055） GLYCEROL × 1 water × 3	Consistent with protein count
2	Insufficient information	Heteromer	Protein 3	Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain × 1 （P08123,P20849） Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain × 1 （P02452,Q14055） GLYCEROL × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CO9A3_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 36–72； UniProt 517–553 Author chain F； PDBConstruct 36–72； UniProt 517–553

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	5cva
Deposition date deposition_date	2015-07-25
Structure title title	Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a1a2a1 of type I collagen
Keywords keywords	collagen, hetero-trimerization, chain stagger, chain register, triple helix, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

5cva__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5cva__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5cva__assembly_2__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	31.92 Å
Rg (electron density)	33.86 Å
Total Rg	33.21 Å
Atom count	1154
Residues	159
Excluded volume	20396 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5cva__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`5cva__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain
Molecular weight formula_weight	7138.7 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D
Atom count atom_count	2572

GSGPPGPPGPPGPPGARGEPGNIGFPGPPGPPGPPGRAPTDQHIKQVCMRVIQEHFAEMAASLKRPDSGAT

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain
Molecular weight formula_weight	6871.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

GSGPPGPPGPPGPPGARGQAGVMGFPGPPGPPGPPGRDATDQHIVDVALKMLQEQLAEVAVSAKREALGAV

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain
Molecular weight formula_weight	6999.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

GSGPPGPPGPPGPPGARGQAGVMGFPGPPGPPGPPGKEASEQRIRELCGGMISEQIAQLAAHLRKPLAPGSI

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	76

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Unit-cell length a length_a	52.410 Å
Unit-cell length b length_b	63.980 Å
Unit-cell length c length_c	65.370 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	112.75 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	2.098 Å
Low-resolution limit resolution_low	48.333 Å
R factor r_factor	0.2382
R_work r_work	0.2341
R_free r_free	0.2785

Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a1a2a1 of type I collagen

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

Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain

State in the Current Structure

Other States of the Same Protein in the Database

Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain

State in the Current Structure

Other States of the Same Protein in the Database

Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain

State in the Current Structure

Other States of the Same Protein in the Database

Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain

State in the Current Structure

Other States of the Same Protein in the Database

Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5cva__assembly_2__model_1

5cva__assembly_2__model_1 | I(q)

5cva__assembly_2__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Citations (1)

Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a1a2a1 of type I collagen

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

Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5cva__assembly_2__model_1

5cva__assembly_2__model_1 | I(q)

5cva__assembly_2__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Citations (1)