SAXSdb — 2j6y

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

PHOSPHOSERINE PHOSPHATASE RSBU

BACILLUS SUBTILIS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RSBU_BACSU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–111； UniProt 1–111 Author chain B； PDBConstruct 1–111； UniProt 1–111 Author chain C； PDBConstruct 1–111； UniProt 1–111 Author chain D； PDBConstruct 1–111； UniProt 1–111 Author chain E； PDBConstruct 1–111； UniProt 1–111

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	2j6y
Deposition date deposition_date	2006-10-05
Structure title title	Structural and Functional Characterisation of partner switching regulating the environmental stress response in Bacillus subtilis
Keywords keywords	HYDROLASE, PARTNER SWITCHING, PROTEIN PHOSPHATASE, RSBT, RSBU, STRESS, BACILLUS SUBTILIS; HYDROLASE
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.

2j6y__assembly_1__model_1

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

Download this curve (.dat)

2j6y__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2j6y__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	16.75 Å
Rg (electron density)	15.32 Å
Total Rg	16.56 Å
Atom count	1400
Residues	166
Excluded volume	25247 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2j6y__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2j6y__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2j6y__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 (2)

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

Domain ID domain_id	d2j6ya_
Class class	a — All alpha proteins
Fold Fold fold	a.186 — KaiA/RbsU domain
Superfamily Superfamily superfamily	a.186.1 — KaiA/RbsU domain
Family Family family	a.186.1.2 — Phosphoserine phosphatase RsbU, N-terminal domain

Domain ID domain_id	d2j6yb_
Class class	a — All alpha proteins
Fold Fold fold	a.186 — KaiA/RbsU domain
Superfamily Superfamily superfamily	a.186.1 — KaiA/RbsU domain
Family Family family	a.186.1.2 — Phosphoserine phosphatase RsbU, N-terminal domain

Domain ID domain_id	d2j6yc_
Class class	a — All alpha proteins
Fold Fold fold	a.186 — KaiA/RbsU domain
Superfamily Superfamily superfamily	a.186.1 — KaiA/RbsU domain
Family Family family	a.186.1.2 — Phosphoserine phosphatase RsbU, N-terminal domain

Domain ID domain_id	d2j6yd_
Class class	a — All alpha proteins
Fold Fold fold	a.186 — KaiA/RbsU domain
Superfamily Superfamily superfamily	a.186.1 — KaiA/RbsU domain
Family Family family	a.186.1.2 — Phosphoserine phosphatase RsbU, N-terminal domain

Domain ID domain_id	d2j6ye_
Class class	a — All alpha proteins
Fold Fold fold	a.186 — KaiA/RbsU domain
Superfamily Superfamily superfamily	a.186.1 — KaiA/RbsU domain
Family Family family	a.186.1.2 — Phosphoserine phosphatase RsbU, N-terminal domain

CATH v4.4 (5 domains)

Domain ID domain_id	2j6yA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1240 — Methyltransferase, Methionine Synthase (B12-binding Domains); Chain A, domain 1
Homologous superfamily homologous superfamily	30 — KaiA/RbsU domain

Domain ID domain_id	2j6yB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1240 — Methyltransferase, Methionine Synthase (B12-binding Domains); Chain A, domain 1
Homologous superfamily homologous superfamily	30 — KaiA/RbsU domain

Domain ID domain_id	2j6yC00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1240 — Methyltransferase, Methionine Synthase (B12-binding Domains); Chain A, domain 1
Homologous superfamily homologous superfamily	30 — KaiA/RbsU domain

Domain ID domain_id	2j6yD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1240 — Methyltransferase, Methionine Synthase (B12-binding Domains); Chain A, domain 1
Homologous superfamily homologous superfamily	30 — KaiA/RbsU domain

Domain ID domain_id	2j6yE00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1240 — Methyltransferase, Methionine Synthase (B12-binding Domains); Chain A, domain 1
Homologous superfamily homologous superfamily	30 — KaiA/RbsU domain

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Unit-cell length a length_a	100.157 Å
Unit-cell length b length_b	47.831 Å
Unit-cell length c length_c	94.968 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	104.36 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	20

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.850 Å
Low-resolution limit resolution_low	42.910 Å
R factor r_factor	0.1860
R_work r_work	0.1830
R_free r_free	0.2530

Description description	PHOSPHOSERINE PHOSPHATASE RSBU
Molecular weight formula_weight	13177.1 kDa
EC 编号 ec_number	3.1.3.3
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	5

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E
Atom count atom_count	3906

Structural and Functional Characterisation of partner switching regulating the environmental stress response in Bacillus subtilis

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

PHOSPHOSERINE PHOSPHATASE RSBU

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

2j6y__assembly_1__model_1

2j6y__assembly_1__model_1 | I(q)

2j6y__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 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

CATH v4.4 (5 domains)

7. Citations (1)

Source organism organism	BACILLUS SUBTILIS
NCBI taxonomy ID ncbi_taxonomy_id	1423
Host organism host_organism	Escherichia coli BL21(DE3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	348

Structural and Functional Characterisation of partner switching regulating the environmental stress response in Bacillus subtilis

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

PHOSPHOSERINE PHOSPHATASE RSBU

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

2j6y__assembly_1__model_1

2j6y__assembly_1__model_1 | I(q)

2j6y__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 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

CATH v4.4 (5 domains)

7. Citations (1)