SAXSdb — 2dsq

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

Insulin-like growth factor-binding protein 4

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Insulin-like growth factor IB × 1 （P05019） Insulin-like growth factor-binding protein 1 × 1 （P08833）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Insulin-like growth factor IB × 1 （P05019） Insulin-like growth factor-binding protein 1 × 1 （P08833）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	IBP4_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–92； UniProt 22–113 Author chain B； PDBConstruct 1–92； UniProt 22–113

Insulin-like growth factor IB

Homo sapiens

UniProt P05019

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Insulin-like growth factor-binding protein 4 × 1 （P22692） Insulin-like growth factor-binding protein 1 × 1 （P08833）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Insulin-like growth factor-binding protein 4 × 1 （P22692） Insulin-like growth factor-binding protein 1 × 1 （P08833）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	IGF1B_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–70； UniProt 49–118 Author chain I； PDBConstruct 1–70； UniProt 49–118

Insulin-like growth factor-binding protein 1

Homo sapiens

UniProt P08833

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Insulin-like growth factor-binding protein 4 × 1 （P22692） Insulin-like growth factor IB × 1 （P05019）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Insulin-like growth factor-binding protein 4 × 1 （P22692） Insulin-like growth factor IB × 1 （P05019）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	IBP1_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain G； PDBConstruct 1–94； UniProt 166–259 Author chain H； PDBConstruct 1–94； UniProt 166–259

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	2dsq
Deposition date deposition_date	2006-07-05
Structure title title	Structural Basis for the Inhibition of Insulin-like Growth Factors by IGF Binding Proteins
Keywords keywords	IGF, IGFBP, Insulin, PROTEIN BINDING-HORMONE-GROWTH FACTOR COMPLEX; PROTEIN BINDING/HORMONE/GROWTH FACTOR
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.

2dsq__assembly_1__model_1

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

Download this curve (.dat)

2dsq__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2dsq__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.49 Å
Rg (electron density)	17.70 Å
Total Rg	18.54 Å
Atom count	1579
Residues	209
Excluded volume	27959 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2dsq__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2dsq__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 (3)

Entity 1 Entity 1 polymer

Description description	Insulin-like growth factor-binding protein 4
Molecular weight formula_weight	9826.5 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,A
Atom count atom_count	3072

DEAIHCPPCSEEKLARCRPPVGCEELVREPGCGCCATCALGLGMPCGVYTPRCGSGLRCYPPRGVEKPLHTLMHGQGVCMELAEIEAIQESL

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 BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Insulin-like growth factor IB
Molecular weight formula_weight	7663.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA

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 BL21(DE3)

Entity 3 Entity 3 polymer

Description description	Insulin-like growth factor-binding protein 1
Molecular weight formula_weight	10878.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,H

VTNIKKWKEPCRIELYRVVESLAKAQETSGEEISKFYLPNCNKNGFYHSRQCETSMDGEAGLCWCVYPWNGKRIPGSPEIRGDPNCQIYFNVQN

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 BL21(DE3)

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d2dsqa_
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.9 — Growth factor receptor domain
Family Family family	g.3.9.1 — Growth factor receptor domain

Domain ID domain_id	d2dsqb_
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.9 — Growth factor receptor domain
Family Family family	g.3.9.1 — Growth factor receptor domain

Domain ID domain_id	d2dsqc_
Class class	g — Small proteins
Fold Fold fold	g.1 — Insulin-like
Superfamily Superfamily superfamily	g.1.1 — Insulin-like
Family Family family	g.1.1.1 — Insulin-like

Domain ID domain_id	d2dsqg1
Class class	g — Small proteins
Fold Fold fold	g.28 — Thyroglobulin type-1 domain
Superfamily Superfamily superfamily	g.28.1 — Thyroglobulin type-1 domain
Family Family family	g.28.1.1 — Thyroglobulin type-1 domain

Domain ID domain_id	d2dsqh_
Class class	g — Small proteins
Fold Fold fold	g.28 — Thyroglobulin type-1 domain
Superfamily Superfamily superfamily	g.28.1 — Thyroglobulin type-1 domain
Family Family family	g.28.1.1 — Thyroglobulin type-1 domain

Domain ID domain_id	d2dsqi_
Class class	g — Small proteins
Fold Fold fold	g.1 — Insulin-like
Superfamily Superfamily superfamily	g.1.1 — Insulin-like
Family Family family	g.1.1.1 — Insulin-like

CATH v4.4 (6 domains)

Domain ID domain_id	2dsqA01
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	40 — Omega-AgatoxinV
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2dsqB01
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	40 — Omega-AgatoxinV
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2dsqC00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily	10 — Insulin-like

Domain ID domain_id	2dsqG00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	800 — Invariant Chain; Chain I
Homologous superfamily homologous superfamily	10 — Thyroglobulin type-1

Domain ID domain_id	2dsqH00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	800 — Invariant Chain; Chain I
Homologous superfamily homologous superfamily	10 — Thyroglobulin type-1

Domain ID domain_id	2dsqI00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily	10 — Insulin-like

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Unit-cell length a length_a	71.280 Å
Unit-cell length b length_b	43.660 Å
Unit-cell length c length_c	81.150 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.67 °
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	2.800 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.2919
R_work r_work	0.2884
R_free r_free	0.3571

Structural Basis for the Inhibition of Insulin-like Growth Factors by IGF Binding Proteins

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

Insulin-like growth factor-binding protein 4

State in the Current Structure

Other States of the Same Protein in the Database

Insulin-like growth factor IB

State in the Current Structure

Other States of the Same Protein in the Database

Insulin-like growth factor-binding protein 1

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

2dsq__assembly_1__model_1

2dsq__assembly_1__model_1 | I(q)

2dsq__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 (3)

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

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)

Structural Basis for the Inhibition of Insulin-like Growth Factors by IGF Binding Proteins

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

Insulin-like growth factor-binding protein 4

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Insulin-like growth factor IB

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Insulin-like growth factor-binding protein 1

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

2dsq__assembly_1__model_1

2dsq__assembly_1__model_1 | I(q)

2dsq__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 (3)

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

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)