SAXSdb — 2a26

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

Calcyclin-binding protein

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	SULFATE ION × 1 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID × 1 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 6	SULFATE ION × 2 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID × 2 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CYBP_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–50； UniProt 1–47 Author chain B； PDBConstruct 4–50； UniProt 1–47 Author chain C； PDBConstruct 4–50； UniProt 1–47

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	2a26
Deposition date deposition_date	2005-06-21
Structure title title	Crystal structure of the N-terminal, dimerization domain of Siah Interacting Protein
Keywords keywords	helical hairpin, dimerization, APOPTOSIS; APOPTOSIS
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.

2a26__assembly_1__model_1

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

Download this curve (.dat)

2a26__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2a26__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	16.41 Å
Rg (electron density)	15.39 Å
Total Rg	16.55 Å
Atom count	785
Residues	94
Excluded volume	14143 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2a26__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2a26__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2a26__assembly_3__model_1`	hexameric （6）	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 (4)

Entity 1 Entity 1 polymer

Description description	Calcyclin-binding protein
Molecular weight formula_weight	5809.7 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	1493

GSHMASEELQKDLEEVKVLLEKATRKRVRDALTAEKSKIETEIKNKMQQK

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 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	3-CYCLOHEXYL-1-PROPYLSULFONIC ACID
Molecular weight formula_weight	221.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	230

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6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d2a26a1
Class class	a — All alpha proteins
Fold Fold fold	a.2 — Long alpha-hairpin
Superfamily Superfamily superfamily	a.2.16 — Calcyclin-binding protein-like
Family Family family	a.2.16.1 — Siah interacting protein N terminal domain-like

Domain ID domain_id	d2a26a2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2a26b2
Class class	a — All alpha proteins
Fold Fold fold	a.2 — Long alpha-hairpin
Superfamily Superfamily superfamily	a.2.16 — Calcyclin-binding protein-like
Family Family family	a.2.16.1 — Siah interacting protein N terminal domain-like

Domain ID domain_id	d2a26b3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2a26c2
Class class	a — All alpha proteins
Fold Fold fold	a.2 — Long alpha-hairpin
Superfamily Superfamily superfamily	a.2.16 — Calcyclin-binding protein-like
Family Family family	a.2.16.1 — Siah interacting protein N terminal domain-like

Domain ID domain_id	d2a26c3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id	2a26A01
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	860 — DNA Excision Repair, Uvrb; Chain A
Homologous superfamily homologous superfamily	10 — UVR domain

Domain ID domain_id	2a26B01
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	860 — DNA Excision Repair, Uvrb; Chain A
Homologous superfamily homologous superfamily	10 — UVR domain

Domain ID domain_id	2a26C01
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	860 — DNA Excision Repair, Uvrb; Chain A
Homologous superfamily homologous superfamily	10 — UVR domain

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Unit-cell length a length_a	58.793 Å
Unit-cell length b length_b	152.609 Å
Unit-cell length c length_c	36.988 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	24

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	1.200 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.1749
R_work r_work	0.1737
R_free r_free	0.1983

Crystal structure of the N-terminal, dimerization domain of Siah Interacting Protein

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

Calcyclin-binding protein

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

2a26__assembly_1__model_1

2a26__assembly_1__model_1 | I(q)

2a26__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (6 domains)

CATH v4.4 (3 domains)

7. Citations (1)

Crystal structure of the N-terminal, dimerization domain of Siah Interacting Protein

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

Calcyclin-binding protein

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

2a26__assembly_1__model_1

2a26__assembly_1__model_1 | I(q)

2a26__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (6 domains)

CATH v4.4 (3 domains)

7. Citations (1)