SAXSdb — 3t7k

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

Regulator of Ty1 transposition protein 107

Saccharomyces cerevisiae

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Histone H2A.1 × 2 （P04911） water × 4	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Histone H2A.1 × 1 （P04911） water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Histone H2A.1 × 1 （P04911） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RT107_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–256； UniProt 820–1070 Author chain B； PDBConstruct 6–256； UniProt 820–1070

Histone H2A.1

OrganismNot specified

UniProt P04911

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Regulator of Ty1 transposition protein 107 × 2 （P38850） water × 4	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Regulator of Ty1 transposition protein 107 × 1 （P38850） water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Regulator of Ty1 transposition protein 107 × 1 （P38850） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	H2A1_YEAST
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–8； UniProt 125–132 Author chain D； PDBConstruct 1–8； UniProt 125–132

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	3t7k
Deposition date deposition_date	2011-07-30
Structure title title	Complex structure of Rtt107p and phosphorylated histone H2A
Keywords keywords	BRCT, DNA repair, phospho-peptide, PROTEIN BINDING; PROTEIN BINDING
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.

3t7k__assembly_1__model_1

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

Download this curve (.dat)

3t7k__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3t7k__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.53 Å
Rg (electron density)	29.08 Å
Total Rg	29.75 Å
Atom count	3871
Residues	475
Excluded volume	70424 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3t7k__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3t7k__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3t7k__assembly_3__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 (3)

Entity 1 Entity 1 polymer

Description description	Regulator of Ty1 transposition protein 107
Molecular weight formula_weight	29388.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3972

GSPHMTKAEKILARFNELPNYDLKAVCTGCFHDGFNEVDIEILNQLGIKIFDNIKETDKLNCIFAPKILRTEKFLKSLSFEPLKFALKPEFIIDLLKQIHSKKDKLSQININLFDYEINGINESIISKTKLPTKVFERANIRCINLVNDIPGGVDTIGSVLKAHGIEKINVLRSKKCTFEDIIPNDVSKQENGGIFKYVLIVTKASQVKKFTKLINDRDKNETILIVEWNWCVESIFHLNVDFTSKKNVLYQKKNN

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	yeast
NCBI taxonomy ID ncbi_taxonomy_id	559292
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Histone H2A.1
Molecular weight formula_weight	927.9 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

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

ATKASQEL

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	101

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	3t7kA01
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	3t7kA02
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	3t7kB01
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	3t7kB02
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	34.517 Å
Unit-cell length b length_b	59.255 Å
Unit-cell length c length_c	85.890 Å
Unit-cell angle α angle_alpha	78.36 °
Unit-cell angle β angle_beta	89.68 °
Unit-cell angle γ angle_gamma	73.17 °
Molecules per unit cell Z z_pdb	2

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.028 Å
Low-resolution limit resolution_low	30.548 Å
R factor r_factor	0.2201
R_work r_work	0.2180
R_free r_free	0.2576

Complex structure of Rtt107p and phosphorylated histone H2A

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

Regulator of Ty1 transposition protein 107

State in the Current Structure

Other States of the Same Protein in the Database

Histone H2A.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

3t7k__assembly_1__model_1

3t7k__assembly_1__model_1 | I(q)

3t7k__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

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)

Complex structure of Rtt107p and phosphorylated histone H2A

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

Regulator of Ty1 transposition protein 107

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Histone H2A.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

3t7k__assembly_1__model_1

3t7k__assembly_1__model_1 | I(q)

3t7k__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

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)