SAXSdb — 9o14

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

Apoptosis regulator Bcl-2,Bcl-2-like protein 1

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 2	stapled BAD BH3 peptide BAD SAHB 4.2 × 1 NICKEL (II) ION × 2 NITRILOTRIACETIC ACID × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	BCL2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–34； UniProt 1–34 Author chain A； PDBConstruct 51–166； UniProt 92–207

Apoptosis regulator Bcl-2,Bcl-2-like protein 1

Homo sapiens

UniProt Q07817

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 2	stapled BAD BH3 peptide BAD SAHB 4.2 × 1 NICKEL (II) ION × 2 NITRILOTRIACETIC ACID × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	B2CL1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 35–50； UniProt 29–44

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	9o14
Deposition date deposition_date	2025-04-03
Structure title title	Crystal Structure of BCL-2 in complex with a stapled BAD BH3 peptide BAD SAHB 4.2
Keywords keywords	Apoptosis regulator, stapled peptide, 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.

9o14__assembly_1__model_1

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

Download this curve (.dat)

9o14__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9o14__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	16.32 Å
Rg (electron density)	14.78 Å
Total Rg	15.94 Å
Atom count	1373
Residues	157
Excluded volume	24032 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9o14__assembly_1__model_1`	dimeric （2）	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	Apoptosis regulator Bcl-2,Bcl-2-like protein 1
Molecular weight formula_weight	19357.6 kDa
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	1477

MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDDVEENRTEAPEGTESEVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMR

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	stapled BAD BH3 peptide BAD SAHB 4.2
Molecular weight formula_weight	2781.2 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

XWLAQRLGRELRRLSDEFVDSFK

Entity 3 Entity 3 non-polymer

Description description	NICKEL (II) ION
Molecular weight formula_weight	58.7 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	NITRILOTRIACETIC ACID
Molecular weight formula_weight	191.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	104

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Unit-cell length a length_a	51.920 Å
Unit-cell length b length_b	58.530 Å
Unit-cell length c length_c	61.570 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.730 Å
Low-resolution limit resolution_low	32.850 Å
R factor r_factor	0.1962
R_work r_work	0.1948
R_free r_free	0.2220

Crystal Structure of BCL-2 in complex with a stapled BAD BH3 peptide BAD SAHB 4.2

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

Apoptosis regulator Bcl-2,Bcl-2-like protein 1

State in the Current Structure

Other States of the Same Protein in the Database

Apoptosis regulator Bcl-2,Bcl-2-like 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

9o14__assembly_1__model_1

9o14__assembly_1__model_1 | I(q)

9o14__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Citations (1)

Crystal Structure of BCL-2 in complex with a stapled BAD BH3 peptide BAD SAHB 4.2

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

Apoptosis regulator Bcl-2,Bcl-2-like 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

Apoptosis regulator Bcl-2,Bcl-2-like 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

9o14__assembly_1__model_1

9o14__assembly_1__model_1 | I(q)

9o14__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Citations (1)