SAXSdb — 1khy

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

CLPB PROTEIN

Escherichia coli

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CLPB_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–148； UniProt 1–148 Author chain B； PDBConstruct 1–148； UniProt 1–148 Author chain C； PDBConstruct 1–148； UniProt 1–148 Author chain D； PDBConstruct 1–148； UniProt 1–148

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	1khy
Deposition date deposition_date	2001-12-01
Structure title title	The Crystal Structure of ClpB N Terminal Domain, Implication to the Peptide Binding Function of ClpB
Keywords keywords	alpha helix, CHAPERONE; 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.

1khy__assembly_1__model_1

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

Download this curve (.dat)

1khy__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1khy__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	15.28 Å
Rg (electron density)	13.74 Å
Total Rg	14.83 Å
Atom count	992
Residues	131
Excluded volume	17641 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1khy__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1khy__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1khy__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1khy__assembly_4__model_1`	monomeric （1）	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) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1khya_
Class class	a — All alpha proteins
Fold Fold fold	a.174 — Double Clp-N motif
Superfamily Superfamily superfamily	a.174.1 — Double Clp-N motif
Family Family family	a.174.1.1 — Double Clp-N motif

Domain ID domain_id	d1khyb_
Class class	a — All alpha proteins
Fold Fold fold	a.174 — Double Clp-N motif
Superfamily Superfamily superfamily	a.174.1 — Double Clp-N motif
Family Family family	a.174.1.1 — Double Clp-N motif

Domain ID domain_id	d1khyc_
Class class	a — All alpha proteins
Fold Fold fold	a.174 — Double Clp-N motif
Superfamily Superfamily superfamily	a.174.1 — Double Clp-N motif
Family Family family	a.174.1.1 — Double Clp-N motif

Domain ID domain_id	d1khyd_
Class class	a — All alpha proteins
Fold Fold fold	a.174 — Double Clp-N motif
Superfamily Superfamily superfamily	a.174.1 — Double Clp-N motif
Family Family family	a.174.1.1 — Double Clp-N motif

CATH v4.4 (4 domains)

Domain ID domain_id	1khyA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1780 — Double Clp-N motif
Homologous superfamily homologous superfamily	10 — Clp, N-terminal domain

Domain ID domain_id	1khyB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1780 — Double Clp-N motif
Homologous superfamily homologous superfamily	10 — Clp, N-terminal domain

Domain ID domain_id	1khyC00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1780 — Double Clp-N motif
Homologous superfamily homologous superfamily	10 — Clp, N-terminal domain

Domain ID domain_id	1khyD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1780 — Double Clp-N motif
Homologous superfamily homologous superfamily	10 — Clp, N-terminal domain

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Unit-cell length a length_a	50.213 Å
Unit-cell length b length_b	52.600 Å
Unit-cell length c length_c	56.841 Å
Unit-cell angle α angle_alpha	90.45 °
Unit-cell angle β angle_beta	111.73 °
Unit-cell angle γ angle_gamma	107.05 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	1.950 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2260
R_work r_work	0.2220
R_free r_free	0.2590

Description description	CLPB PROTEIN
Molecular weight formula_weight	15919.5 kDa
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	4304

The Crystal Structure of ClpB N Terminal Domain, Implication to the Peptide Binding Function of ClpB

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

CLPB 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

1khy__assembly_1__model_1

1khy__assembly_1__model_1 | I(q)

1khy__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) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
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	254

The Crystal Structure of ClpB N Terminal Domain, Implication to the Peptide Binding Function of ClpB

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

CLPB 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

1khy__assembly_1__model_1

1khy__assembly_1__model_1 | I(q)

1khy__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) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)