SAXSdb — 3vz8

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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 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

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 A； PDBConstruct 14–199； UniProt 191–376 Author chain B； PDBConstruct 14–199； UniProt 191–376 Author chain C； PDBConstruct 14–199； UniProt 191–376

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	3vz8
Deposition date deposition_date	2012-10-09
Structure title title	Crystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro 187, Arg 188 and Ser 190 replaced with all Gly
Keywords keywords	Chaperon, HSP60, GroEL, Cell division, ATP-binding, Phosphorylation, 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.

3vz8__assembly_1__model_1

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

Download this curve (.dat)

3vz8__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3vz8__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	17.53 Å
Rg (electron density)	16.29 Å
Total Rg	17.27 Å
Atom count	1401
Residues	185
Excluded volume	25219 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3vz8__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3vz8__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3vz8__assembly_3__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) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d3vz8a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.8 — The 'swivelling' beta/beta/alpha domain
Superfamily Superfamily superfamily	c.8.5 — GroEL apical domain-like
Family Family family	c.8.5.1 — GroEL-like chaperone, apical domain

Domain ID domain_id	d3vz8b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.8 — The 'swivelling' beta/beta/alpha domain
Superfamily Superfamily superfamily	c.8.5 — GroEL apical domain-like
Family Family family	c.8.5.1 — GroEL-like chaperone, apical domain

Domain ID domain_id	d3vz8c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.8 — The 'swivelling' beta/beta/alpha domain
Superfamily Superfamily superfamily	c.8.5 — GroEL apical domain-like
Family Family family	c.8.5.1 — GroEL-like chaperone, apical domain

CATH v4.4 (3 domains)

Domain ID domain_id	3vz8A00
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	7 — GroEL
Homologous superfamily homologous superfamily	10 — GroEL

Domain ID domain_id	3vz8B00
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	7 — GroEL
Homologous superfamily homologous superfamily	10 — GroEL

Domain ID domain_id	3vz8C00
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	7 — GroEL
Homologous superfamily homologous superfamily	10 — GroEL

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Unit-cell length a length_a	95.058 Å
Unit-cell length b length_b	38.010 Å
Unit-cell length c length_c	102.204 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	116.23 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	6

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

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	47.510 Å
R factor r_factor	0.2630
R_work r_work	0.2630
R_free r_free	0.2720

Description description	60 kDa chaperonin
Molecular weight formula_weight	21359.4 kDa
Source method src_method	man
Copy count entity_count	3

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	4396

Crystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro 187, Arg 188 and Ser 190 replaced with all Gly

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

3vz8__assembly_1__model_1

3vz8__assembly_1__model_1 | I(q)

3vz8__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) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)

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

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	193

Crystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro 187, Arg 188 and Ser 190 replaced with all Gly

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

3vz8__assembly_1__model_1

3vz8__assembly_1__model_1 | I(q)

3vz8__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) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)