SAXSdb — 2w9r

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

ATP-DEPENDENT CLP PROTEASE ADAPTER PROTEIN CLPS

ESCHERICHIA COLI

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	DNA PROTECTION DURING STARVATION PROTEIN × 1 （P0ABT2） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CLPS_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–106； UniProt 1–106

DNA PROTECTION DURING STARVATION PROTEIN

ESCHERICHIA COLI

UniProt P0ABT2

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	ATP-DEPENDENT CLP PROTEASE ADAPTER PROTEIN CLPS × 1 （P0A8Q6） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DPS_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–11； UniProt 6–16

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	2w9r
Deposition date deposition_date	2009-01-28
Structure title title	Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS
Keywords keywords	;CHAPERONE, ADAPTOR PROTEIN, DNA CONDENSATION, IRON, CLPS, CLPA, CYTOPLASM, N-END RULE, DNA-BINDING, IRON STORAGE, METAL-BINDING, OXIDOREDUCTASE ;; CHAPERONE
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.

2w9r__assembly_1__model_1

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

Download this curve (.dat)

2w9r__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2w9r__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.99 Å
Rg (electron density)	19.19 Å
Total Rg	19.82 Å
Atom count	856
Residues	108
Excluded volume	15527 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2w9r__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 (3)

Entity 1 Entity 1 polymer

Description description	ATP-DEPENDENT CLP PROTEASE ADAPTER PROTEIN CLPS
Molecular weight formula_weight	12321.2 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	929

MGKTNDWLDFDQLAEEKVRDALKPPSMYKVILVNDDYTPMEFVIDVLQKFFSYDVERATQLMLAVHYQGKAICGVFTAEVAETKVAMVNKYARENEHPLLCTLEKAGA

Source Source

Source organism organism	ESCHERICHIA COLI
NCBI taxonomy ID ncbi_taxonomy_id	83333
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	DNA PROTECTION DURING STARVATION PROTEIN
Molecular weight formula_weight	1251.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

LVKSKATNLLY

Source Source

Source organism organism	ESCHERICHIA COLI
NCBI taxonomy ID ncbi_taxonomy_id	83333
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	68

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2w9ra_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.45 — ClpS-like
Superfamily Superfamily superfamily	d.45.1 — ClpS-like
Family Family family	d.45.1.2 — Adaptor protein ClpS (YljA)

CATH v4.4 (1 domains)

Domain ID domain_id	2w9rA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1390 — Ribosomal Protein L30; Chain: A,
Homologous superfamily homologous superfamily	10 — Ribosomal protein L7/L12, C-terminal domain/Adaptor protein ClpS

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Unit-cell length a length_a	28.080 Å
Unit-cell length b length_b	28.230 Å
Unit-cell length c length_c	38.910 Å
Unit-cell angle α angle_alpha	97.44 °
Unit-cell angle β angle_beta	106.45 °
Unit-cell angle γ angle_gamma	92.39 °
Molecules per unit cell Z z_pdb	1

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

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	25.000 Å
R factor r_factor	0.2280
R_work r_work	0.2260
R_free r_free	0.2540

Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS

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

ATP-DEPENDENT CLP PROTEASE ADAPTER PROTEIN CLPS

State in the Current Structure

Other States of the Same Protein in the Database

DNA PROTECTION DURING STARVATION PROTEIN

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

2w9r__assembly_1__model_1

2w9r__assembly_1__model_1 | I(q)

2w9r__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

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS

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

ATP-DEPENDENT CLP PROTEASE ADAPTER PROTEIN CLPS

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

DNA PROTECTION DURING STARVATION 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

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2w9r__assembly_1__model_1

2w9r__assembly_1__model_1 | I(q)

2w9r__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

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)