3coj

Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1

Method: X-RAY DIFFRACTION

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

Breast cancer type 1 susceptibility protein

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Acetyl-CoA carboxylase 1 × 1 （Q13085）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Acetyl-CoA carboxylase 1 × 1 （Q13085）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Acetyl-CoA carboxylase 1 × 1 （Q13085）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Acetyl-CoA carboxylase 1 × 1 （Q13085）	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	Acetyl-CoA carboxylase 1 × 1 （Q13085）	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	Acetyl-CoA carboxylase 1 × 1 （Q13085）	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 2	Acetyl-CoA carboxylase 1 × 1 （Q13085）	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 2	Acetyl-CoA carboxylase 1 × 1 （Q13085）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	BRCA1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 22–235； UniProt 1646–1859 Author chain B； PDBConstruct 22–235； UniProt 1646–1859 Author chain C； PDBConstruct 22–235； UniProt 1646–1859 Author chain D； PDBConstruct 22–235； UniProt 1646–1859 Author chain E； PDBConstruct 22–235； UniProt 1646–1859 Author chain F； PDBConstruct 22–235； UniProt 1646–1859 Author chain G； PDBConstruct 22–235； UniProt 1646–1859 Author chain X； PDBConstruct 22–235； UniProt 1646–1859

Acetyl-CoA carboxylase 1

OrganismNot specified

UniProt Q13085

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Breast cancer type 1 susceptibility protein × 1 （P38398）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Breast cancer type 1 susceptibility protein × 1 （P38398）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Breast cancer type 1 susceptibility protein × 1 （P38398）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Breast cancer type 1 susceptibility protein × 1 （P38398）	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	Breast cancer type 1 susceptibility protein × 1 （P38398）	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	Breast cancer type 1 susceptibility protein × 1 （P38398）	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 2	Breast cancer type 1 susceptibility protein × 1 （P38398）	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 2	Breast cancer type 1 susceptibility protein × 1 （P38398）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ACACA_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain H； PDBConstruct 1–13； UniProt 1258–1270 Author chain I； PDBConstruct 1–13； UniProt 1258–1270 Author chain J； PDBConstruct 1–13； UniProt 1258–1270 Author chain K； PDBConstruct 1–13； UniProt 1258–1270 Author chain L； PDBConstruct 1–13； UniProt 1258–1270 Author chain M； PDBConstruct 1–13； UniProt 1258–1270 Author chain N； PDBConstruct 1–13； UniProt 1258–1270 Author chain O； PDBConstruct 1–13； UniProt 1258–1270

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	3coj
Deposition date deposition_date	2008-03-28
Structure title title	Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1
Keywords keywords	;Breast Cancer, Ovarian Cancer, Fatty Acid Biosynthesis, lipid synthesis, Obesity, Protein-peptide complex, Protein Protein interaction, Anti-oncogene, Cell cycle, Disease mutation, DNA damage, DNA repair, DNA-binding, Metal-binding, Nucleus, Phosphoprotein, Zinc-finger, Alternative promoter usage, ATP-binding, Biotin, Ligase, Manganese, Multifunctional enzyme, Nucleotide-binding, ANTITUMOR PROTEIN-LIGASE COMPLEX ;; ANTITUMOR PROTEIN/LIGASE
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.

3coj__assembly_2__model_1

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

Download this curve (.dat)

3coj__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3coj__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	19.49 Å
Rg (electron density)	18.84 Å
Total Rg	19.75 Å
Atom count	1746
Residues	217
Excluded volume	31213 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3coj__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3coj__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3coj__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`3coj__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`3coj__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`3coj__assembly_6__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`3coj__assembly_7__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`3coj__assembly_8__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 (2)

Entity 1 Entity 1 polymer

Description description	Breast cancer type 1 susceptibility protein
Molecular weight formula_weight	26833.8 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	X,A,B,C,D,E,F,G
Atom count atom_count	13867

MGSSHHHHHHSSGLVPRGSHMVNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIP

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	Acetyl-CoA carboxylase 1
Molecular weight formula_weight	1409.3 kDa
EC 编号 ec_number	6.4.1.2
Source method src_method	syn
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,I,J,K,L,M,N,O

DSPPQSPTFPEAG

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6. Fold Classification (SCOP + CATH) 32 domains

SCOP 2.08 (16 domains)

Domain ID domain_id	d3coja1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3coja2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3cojb1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3cojb2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3cojc1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3cojc2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3cojd1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3cojd2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3coje1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3coje2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3cojf1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3cojf2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3cojg1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3cojg2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3cojx1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

Domain ID domain_id	d3cojx2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.15 — BRCT domain
Superfamily Superfamily superfamily	c.15.1 — BRCT domain
Family Family family	c.15.1.3 — BRCT domain

CATH v4.4 (16 domains)

Domain ID domain_id	3cojA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojC01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojC02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojD01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojD02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojE01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojE02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojF01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojF02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojG01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojG02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojX01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

Domain ID domain_id	3cojX02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10190 — BRCT domain

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Unit-cell length a length_a	83.330 Å
Unit-cell length b length_b	181.513 Å
Unit-cell length c length_c	194.643 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	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	3.210 Å
Low-resolution limit resolution_low	29.890 Å
R factor r_factor	0.2597
R_work r_work	0.2571
R_free r_free	0.3075

Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1

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

Breast cancer type 1 susceptibility protein

State in the Current Structure

Other States of the Same Protein in the Database

Acetyl-CoA carboxylase 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

3coj__assembly_2__model_1

3coj__assembly_2__model_1 | I(q)

3coj__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 32 domains

SCOP 2.08 (16 domains)

CATH v4.4 (16 domains)

7. Citations (1)

Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1

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

Breast cancer type 1 susceptibility 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

Acetyl-CoA carboxylase 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

3coj__assembly_2__model_1

3coj__assembly_2__model_1 | I(q)

3coj__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 32 domains

SCOP 2.08 (16 domains)

CATH v4.4 (16 domains)

7. Citations (1)