SAXSdb — 29hb

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

ATP-dependent Clp protease proteolytic subunit

Enterobacter

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 21	unknown substrate bound to ClpE/ClpP × 1 ATP-dependent Clp protease, ATP-binding subunit ClpE × 6 （Q837W9） ADENOSINE-5'-TRIPHOSPHATE × 10	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CLPP_ENTFA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–197； UniProt 1–197 Author chain B； PDBConstruct 1–197； UniProt 1–197 Author chain C； PDBConstruct 1–197； UniProt 1–197 Author chain D； PDBConstruct 1–197； UniProt 1–197 Author chain E； PDBConstruct 1–197； UniProt 1–197 Author chain F； PDBConstruct 1–197； UniProt 1–197 Author chain G； PDBConstruct 1–197； UniProt 1–197 Author chain I； PDBConstruct 1–197； UniProt 1–197 Author chain K； PDBConstruct 1–197； UniProt 1–197 Author chain L； PDBConstruct 1–197； UniProt 1–197 Author chain M； PDBConstruct 1–197； UniProt 1–197 Author chain N； PDBConstruct 1–197； UniProt 1–197 Author chain S； PDBConstruct 1–197； UniProt 1–197 Author chain T； PDBConstruct 1–197； UniProt 1–197

ATP-dependent Clp protease, ATP-binding subunit ClpE

Enterobacter

UniProt Q837W9

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 21	ATP-dependent Clp protease proteolytic subunit × 14 （Q837R0） unknown substrate bound to ClpE/ClpP × 1 ADENOSINE-5'-TRIPHOSPHATE × 10	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q837W9_ENTFA
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain a； PDBConstruct 1–746； UniProt 5–750 Author chain b； PDBConstruct 1–746； UniProt 5–750 Author chain c； PDBConstruct 1–746； UniProt 5–750 Author chain d； PDBConstruct 1–746； UniProt 5–750 Author chain e； PDBConstruct 1–746； UniProt 5–750 Author chain f； PDBConstruct 1–746； UniProt 5–750

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	29hb
Deposition date deposition_date	2026-03-11
Structure title title	Cryo-EM structure of the ClpE/ClpP degradation complex from E.faecalis
Keywords keywords	AAA+ chaperone, protease, CHAPERONE; CHAPERONE
Experimental Method method	ELECTRON MICROSCOPY

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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.

29hb__assembly_1__model_1

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

Download this curve (.dat)

29hb__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

29hb__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	63.44 Å
Rg (electron density)	63.36 Å
Total Rg	63.41 Å
Atom count	46198
Residues	5969
Excluded volume	821190 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`29hb__assembly_1__model_1`	21-meric （21）	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 (4)

Entity 1 Entity 1 polymer

Description description	ATP-dependent Clp protease proteolytic subunit
Molecular weight formula_weight	21640.5 kDa
EC 编号 ec_number	3.4.21.92
Source method src_method	man
Copy count entity_count	14

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,I,K,L,M,N,S,T
Atom count atom_count	46198

MNLIPTVIEQSSRGERAYDIYSRLLKDRIIMLSGPIDDNVANSVIAQLLFLDAQDSEKDIYLYINSPGGSVSAGLAIFDTMNFVKADVQTIVLGMAASMGSFLLTAGQKGKRFALPNAEIMIHQPLGGAQGQATEIEIAARHILDTRQRLNSILAERTGQPIEVIERDTDRDNYMTAEQAKEYGLIDEVMENSSALN

Source Source

Source organism organism	Enterobacter
NCBI taxonomy ID ncbi_taxonomy_id	547
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	unknown substrate bound to ClpE/ClpP
Molecular weight formula_weight	1379.7 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

XXXXXXXXXXXXXXXX

Entity 3 Entity 3 polymer

Description description	ATP-dependent Clp protease, ATP-binding subunit ClpE
Molecular weight formula_weight	82590.0 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	b,c,d,a,e,f

MICQNCQQNEATIHLYANVNGQRKQLDYCQSCYQKLKNQANNSPQNMGQDPFGFGSLDDLYRSLSRQMQQGNPYEQQTPPTQFGDGGNGGQPPRGGAGAGQGLLGEYGINITEAARQGDIDPVVGRDQEIKRVIEILNRRTKNNPVLIGEPGVGKTAVVEGLAQKIVDGDVPQKLLDKEVIRLDVVSLVQGTGIRGQFEERMQKLIEEITEAENVILFIDEVHEIVGAGAAGDGNMDAGNILKPALARGELQLVGATTLNEYRIIEKDAALERRMQPVQVDEPTVAETITILHGLQKRYEDYHHVKYTDEAINAAANLSNRYIQDRFLPDKAIDLLDESGSKMNLTIQLVDPKTIDKKLAEAEQQKQQASAEEDFEKAAYYRDQINKLQAMKEKQISDEETPVITEKDIEAIVEQKTGIPVGDLKEKEQTQLKNLAVDLKAHVVGQDDAVDKVAKAIRRNRVGLGKQNRPIGSFLFVGPTGVGKTELAKQLAFELFGSEDSMVRFDMSEYMEKHSVSKLIGSPPGYVGYDEAGQLTEKVRRNPYSLILLDEVEKAHPDVLHMFLQILDDGRLTDAQGRTVSFKDTIIIMTSNAGTGAVEANVGFGAAREGVTKSVLGQLNNFFTPEFLNRFDGIIEFKALSKENLMNIVSLMLEEVNSLLAKQKLHIEVPTEVKEKLVDLGYDPAMGARPLRRTIQEQIEDGIAEYYLDHPENHQLVAALDNEGKIIVTGAQEVTKTETSTSDQAE

Source Source

Source organism organism	Enterobacter
NCBI taxonomy ID ncbi_taxonomy_id	547
Host organism host_organism	Escherichia coli

Entity 4 Entity 4 non-polymer

Description description	ADENOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	507.2 kDa
Source method src_method	syn
Copy count entity_count	10

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

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

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	2.80 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	556680

Cryo-EM structure of the ClpE/ClpP degradation complex from E.faecalis

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

ATP-dependent Clp protease proteolytic subunit

State in the Current Structure

Other States of the Same Protein in the Database

ATP-dependent Clp protease, ATP-binding subunit ClpE

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

29hb__assembly_1__model_1

29hb__assembly_1__model_1 | I(q)

29hb__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

7. Citations (1)

Cryo-EM structure of the ClpE/ClpP degradation complex from E.faecalis

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

ATP-dependent Clp protease proteolytic subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

ATP-dependent Clp protease, ATP-binding subunit ClpE

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

29hb__assembly_1__model_1

29hb__assembly_1__model_1 | I(q)

29hb__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

7. Citations (1)