SAXSdb — 4v43

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

GROEL PROTEIN

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 14	No other associated polymer	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 14	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CH60_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 1–547； UniProt 1–547 Author chain 2； PDBConstruct 1–547； UniProt 1–547 Author chain A； PDBConstruct 1–547； UniProt 1–547 Author chain B； PDBConstruct 1–547； UniProt 1–547 Author chain C； PDBConstruct 1–547； UniProt 1–547 Author chain D； PDBConstruct 1–547； UniProt 1–547 Author chain E； PDBConstruct 1–547； UniProt 1–547 Author chain F； PDBConstruct 1–547； UniProt 1–547 Author chain G； PDBConstruct 1–547； UniProt 1–547 Author chain H； PDBConstruct 1–547； UniProt 1–547 Author chain I； PDBConstruct 1–547； UniProt 1–547 Author chain J； PDBConstruct 1–547； UniProt 1–547 Author chain K； PDBConstruct 1–547； UniProt 1–547 Author chain L； PDBConstruct 1–547； UniProt 1–547 Author chain M； PDBConstruct 1–547； UniProt 1–547 Author chain N； PDBConstruct 1–547； UniProt 1–547 Author chain O； PDBConstruct 1–547； UniProt 1–547 Author chain P； PDBConstruct 1–547； UniProt 1–547 Author chain Q； PDBConstruct 1–547； UniProt 1–547 Author chain R； PDBConstruct 1–547； UniProt 1–547 Author chain S； PDBConstruct 1–547； UniProt 1–547 Author chain T； PDBConstruct 1–547； UniProt 1–547 Author chain U； PDBConstruct 1–547； UniProt 1–547 Author chain V； PDBConstruct 1–547； UniProt 1–547 Author chain W； PDBConstruct 1–547； UniProt 1–547 Author chain X； PDBConstruct 1–547； UniProt 1–547 Author chain Y； PDBConstruct 1–547； UniProt 1–547 Author chain Z； PDBConstruct 1–547； UniProt 1–547

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	4v43
Deposition date deposition_date	2002-01-02
Structure title title	Structural and mechanistic basis for allostery in the bacterial chaperonin GroEL
Keywords keywords	Wild Type GroEL, ALLOSTERY, 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.

4v43__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

4v43__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4v43__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	65.55 Å
Rg (electron density)	64.34 Å
Total Rg	64.45 Å
Atom count	53998
Residues	7350
Excluded volume	968170 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4v43__assembly_1__model_1`	tetradecameric （14）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`4v43__assembly_2__model_1`	tetradecameric （14）	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 (1)

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Unit-cell length a length_a	137.666 Å
Unit-cell length b length_b	264.235 Å
Unit-cell length c length_c	294.799 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	92.39 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	56

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	3.520 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.2910
R_free r_free	0.2980

Description description	GROEL PROTEIN
Molecular weight formula_weight	57158.5 kDa
Mutation mutation	D398A
Source method src_method	man
Copy count entity_count	28

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,1,2
Atom count atom_count	107996

Structural and mechanistic basis for allostery in the bacterial chaperonin GroEL

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

GROEL 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

4v43__assembly_2__model_1

4v43__assembly_2__model_1 | I(q)

4v43__assembly_2__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

7. Citations (5)

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Structural and mechanistic basis for allostery in the bacterial chaperonin GroEL

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

GROEL 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

4v43__assembly_2__model_1

4v43__assembly_2__model_1 | I(q)

4v43__assembly_2__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

7. Citations (5)