1gr5

Solution Structure of apo GroEL by Cryo-Electron microscopy

Method: ELECTRON MICROSCOPY

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

60 KDA CHAPERONIN

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CH60_ECOL6
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–547； UniProt 2–548 Author chain B； PDBConstruct 1–547； UniProt 2–548 Author chain C； PDBConstruct 1–547； UniProt 2–548 Author chain D； PDBConstruct 1–547； UniProt 2–548 Author chain E； PDBConstruct 1–547； UniProt 2–548 Author chain F； PDBConstruct 1–547； UniProt 2–548 Author chain G； PDBConstruct 1–547； UniProt 2–548 Author chain H； PDBConstruct 1–547； UniProt 2–548 Author chain I； PDBConstruct 1–547； UniProt 2–548 Author chain J； PDBConstruct 1–547； UniProt 2–548 Author chain K； PDBConstruct 1–547； UniProt 2–548 Author chain L； PDBConstruct 1–547； UniProt 2–548 Author chain M； PDBConstruct 1–547； UniProt 2–548 Author chain N； PDBConstruct 1–547； UniProt 2–548

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	1gr5
Deposition date deposition_date	2001-12-14
Structure title title	Solution Structure of apo GroEL by Cryo-Electron microscopy
Keywords keywords	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.

1gr5__assembly_1__model_1

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

Download this curve (.dat)

1gr5__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1gr5__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	64.41 Å
Rg (electron density)	63.28 Å
Total Rg	63.37 Å
Atom count	52668
Residues	7238
Excluded volume	947720 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1gr5__assembly_1__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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6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (14 domains)

Domain ID domain_id	d1gr5a_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5b_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5c_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5d_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5e_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5f_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5g_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5h_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5i_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5j_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5k_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5l_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5m_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

Domain ID domain_id	d1gr5n_
Class class	i — Low resolution protein structures
Fold Fold fold	i.16 — GroE chaperon
Superfamily Superfamily superfamily	i.16.1 — GroE chaperon
Family Family family	i.16.1.1 — GroE chaperon

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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	1

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

Resolution resolution	7.900 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	7.90 Å
Resolution测定Method resolution_method	MODEL-BASED ANGULAR REFINEMENT
颗粒数 num_particles	8728

Description description	60 KDA CHAPERONIN
Molecular weight formula_weight	57188.4 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	14

Solution Structure of apo GroEL by Cryo-Electron microscopy

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

60 KDA CHAPERONIN

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

1gr5__assembly_1__model_1

1gr5__assembly_1__model_1 | I(q)

1gr5__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (14 domains)

7. Citations (4)

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N
Atom count atom_count	52668

Source organism organism	ESCHERICHIA COLI
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	ESCHERICHIA COLI

Solution Structure of apo GroEL by Cryo-Electron microscopy

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

60 KDA CHAPERONIN

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

1gr5__assembly_1__model_1

1gr5__assembly_1__model_1 | I(q)

1gr5__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (14 domains)

7. Citations (4)