1iyj

STRUCTURE OF A BRCA2-DSS1 COMPLEX

Method: X-RAY DIFFRACTION

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

Deleted in split hand/split foot protein 1

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	breast cancer susceptibility × 1 （O35923）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	breast cancer susceptibility × 1 （O35923）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DSS1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–70； UniProt 1–70 Author chain C； PDBConstruct 1–70； UniProt 1–70

breast cancer susceptibility

Rattus norvegicus

UniProt O35923

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Deleted in split hand/split foot protein 1 × 1 （P60896）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Deleted in split hand/split foot protein 1 × 1 （P60896）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	BRCA2_RAT
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–817； UniProt 2335–3151 Author chain D； PDBConstruct 1–817； UniProt 2335–3151

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	1iyj
Deposition date deposition_date	2002-08-28
Structure title title	STRUCTURE OF A BRCA2-DSS1 COMPLEX
Keywords keywords	TUMOR SUPPRESSOR, BREAST CANCER SUSCEPTIBILITY, DNA-BINDING, GENE REGULATION-ANTITUMOR PROTEIN COMPLEX; GENE REGULATION/ANTITUMOR 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.

1iyj__assembly_1__model_1

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

Download this curve (.dat)

1iyj__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1iyj__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	34.84 Å
Rg (electron density)	35.25 Å
Total Rg	35.52 Å
Atom count	5046
Residues	636
Excluded volume	89958 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1iyj__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1iyj__assembly_2__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	Deleted in split hand/split foot protein 1
Molecular weight formula_weight	8284.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	10092

MSEKKQPVDLGLLEEDDEFEEFPAEDWAGLDEDEDAHVWEDNWDDDNVEDDFSNQLRAELEKHGYKMETS

Source Source

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

Entity 2 Entity 2 polymer

Description description	breast cancer susceptibility
Molecular weight formula_weight	91724.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

SSNPTVSALRSERTRHSVSDKSTKVFVPPFKVKSRFHRDEHFDSKNVNLEGKNQKSADGVSEDGNDSDFPQFNKDLMSSLQNARDLQDIRIKNKERHHLCPQPGSLYLTKSSTLPRISLQAAVGDSVPSACSPKQLYMYGVSKACISVNSKNAEYFQFAIEDHFGKEALCAGKGFRLADGGWLIPSDDGKAGKEEFYRALCDTPGVDPKLISSVWVSNHYRWIVWKLAAMEFAFPKEFANRCLNPERVLLQLKYRYDVEIDNSSRSALKKILERDDTAAKTLVLCVSDIISLSTNVSETSGSKASSEDSNKVDTIELTDGWYAVKAQLDPPLLALVKSGRLTVGQKIITQGAELVGSPDACAPLEAPDSLRLKISANSTRPARWHSKLGFFHDPRPFPLPLSSLFSDGGNVGCVDVIVQRVYPLQWVEKTVSGSYIFRNEREEEKEALRFAEAQQKKLEALFTKVHTELKEHEEDIAQRRVLSRALTRQQVHALQDGAELYAAVQDASDPEHLETCFSEEQLRALNNYRQMLSDKKQARIQSEFRKALEAAEKEEGLSRDVSTVWKLRVTSYKKREKSALLSIWRPSSDLPSLLTEGQRYRIYHLSVSKSKNKFEWPSIQLTATKRTQYQQLPVSSETLLQLYQPRELLPFSKLSDPAFQPPCSEVDVVGVVVSVVKPIGLAPLVYLSDECLHLLVVKFGIDLNEDIKPRVLIAASNLQWRPESTSRVPTLFAGNFSVFSASPKEAHFQERVTNMKHAIENIDTFYKEAEKKLIQVLKGDSPKWSTPNKDPTREPYPASTCSASDLASGGQLPRSSP

Source Source

Source organism organism	Rattus norvegicus
Common name common_name	Norway rat
NCBI taxonomy ID ncbi_taxonomy_id	10116
Host organism host_organism	Spodoptera frugiperda

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6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (10 domains)

Domain ID domain_id	d1iyjb1
Class class	a — All alpha proteins
Fold Fold fold	a.170 — BRCA2 helical domain
Superfamily Superfamily superfamily	a.170.1 — BRCA2 helical domain
Family Family family	a.170.1.1 — BRCA2 helical domain

Domain ID domain_id	d1iyjb2
Class class	a — All alpha proteins
Fold Fold fold	a.171 — BRCA2 tower domain
Superfamily Superfamily superfamily	a.171.1 — BRCA2 tower domain
Family Family family	a.171.1.1 — BRCA2 tower domain

Domain ID domain_id	d1iyjb3
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.4 — Nucleic acid-binding proteins
Family Family family	b.40.4.3 — Single strand DNA-binding domain, SSB

Domain ID domain_id	d1iyjb4
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.4 — Nucleic acid-binding proteins
Family Family family	b.40.4.3 — Single strand DNA-binding domain, SSB

Domain ID domain_id	d1iyjb5
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.4 — Nucleic acid-binding proteins
Family Family family	b.40.4.3 — Single strand DNA-binding domain, SSB

Domain ID domain_id	d1iyjd1
Class class	a — All alpha proteins
Fold Fold fold	a.170 — BRCA2 helical domain
Superfamily Superfamily superfamily	a.170.1 — BRCA2 helical domain
Family Family family	a.170.1.1 — BRCA2 helical domain

Domain ID domain_id	d1iyjd2
Class class	a — All alpha proteins
Fold Fold fold	a.171 — BRCA2 tower domain
Superfamily Superfamily superfamily	a.171.1 — BRCA2 tower domain
Family Family family	a.171.1.1 — BRCA2 tower domain

Domain ID domain_id	d1iyjd3
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.4 — Nucleic acid-binding proteins
Family Family family	b.40.4.3 — Single strand DNA-binding domain, SSB

Domain ID domain_id	d1iyjd4
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.4 — Nucleic acid-binding proteins
Family Family family	b.40.4.3 — Single strand DNA-binding domain, SSB

Domain ID domain_id	d1iyjd5
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.4 — Nucleic acid-binding proteins
Family Family family	b.40.4.3 — Single strand DNA-binding domain, SSB

CATH v4.4 (6 domains)

Domain ID domain_id	1iyjB02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	1iyjB03
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	1iyjB04
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	1iyjD02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	1iyjD03
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	1iyjD04
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

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Unit-cell length a length_a	130.314 Å
Unit-cell length b length_b	130.314 Å
Unit-cell length c length_c	192.615 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	8

Space group space_group	P 43
Space-group number int_tables_number	78
Crystal system crystal_system	—

Resolution resolution	3.400 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2480
R_work r_work	0.2440
R_free r_free	0.2950

STRUCTURE OF A BRCA2-DSS1 COMPLEX

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

Deleted in split hand/split foot protein 1

State in the Current Structure

Other States of the Same Protein in the Database

breast cancer susceptibility

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

1iyj__assembly_1__model_1

1iyj__assembly_1__model_1 | I(q)

1iyj__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 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (10 domains)

CATH v4.4 (6 domains)

7. Citations (1)

STRUCTURE OF A BRCA2-DSS1 COMPLEX

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

Deleted in split hand/split foot 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

breast cancer susceptibility

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

1iyj__assembly_1__model_1

1iyj__assembly_1__model_1 | I(q)

1iyj__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 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (10 domains)

CATH v4.4 (6 domains)

7. Citations (1)