SAXSdb — 5nb2

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

Collagen alpha-2(IV) chain

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CO4A2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–228； UniProt 1485–1712 Author chain B； PDBConstruct 1–228； UniProt 1485–1712

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	5nb2
Deposition date deposition_date	2017-02-28
Structure title title	Crystal structures of homooligomers of collagen type IV. alpha2NC1
Keywords keywords	Non-collagenous domain of collagen type IV. A principal structural component of basement membranes, 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.

5nb2__assembly_1__model_1

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

Download this curve (.dat)

5nb2__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5nb2__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.47 Å
Rg (electron density)	28.26 Å
Total Rg	29.09 Å
Atom count	5788
Residues	764
Excluded volume	102910 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5nb2__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`5nb2__assembly_2__model_1`	tetrameric （4）	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 (2)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d5nb2a1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.6 — Noncollagenous (NC1) domain of collagen IV

Domain ID domain_id	d5nb2b1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.6 — Noncollagenous (NC1) domain of collagen IV

CATH v4.4 (2 domains)

Domain ID domain_id	5nb2A00
Class class	2 — Mainly Beta
Architecture architecture	170 — Beta Complex
Topology topology	240 — Noncollagenous (NC1) domain of collagen IV
Homologous superfamily homologous superfamily	10 — Collagen IV, non-collagenous

Domain ID domain_id	5nb2B00
Class class	2 — Mainly Beta
Architecture architecture	170 — Beta Complex
Topology topology	240 — Noncollagenous (NC1) domain of collagen IV
Homologous superfamily homologous superfamily	10 — Collagen IV, non-collagenous

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Unit-cell length a length_a	94.330 Å
Unit-cell length b length_b	94.330 Å
Unit-cell length c length_c	225.618 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	32

Space group space_group	I 4 2 2
Space-group number int_tables_number	97
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	112.810 Å
R factor r_factor	0.2477
R_work r_work	0.2461
R_free r_free	0.2794

Description description	Collagen alpha-2(IV) chain
Molecular weight formula_weight	25114.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2794

Crystal structures of homooligomers of collagen type IV. alpha2NC1

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

Collagen alpha-2(IV) 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

5nb2__assembly_1__model_1

5nb2__assembly_1__model_1 | I(q)

5nb2__assembly_1__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Spodoptera frugiperda

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	55

Crystal structures of homooligomers of collagen type IV. alpha2NC1

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

Collagen alpha-2(IV) 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

5nb2__assembly_1__model_1

5nb2__assembly_1__model_1 | I(q)

5nb2__assembly_1__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)