1sjp

Mycobacterium tuberculosis Chaperonin60.2

Method: X-RAY DIFFRACTION

▼

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

60 kDa chaperonin 2

Mycobacterium tuberculosis

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CH602_MYCTU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–498； UniProt 42–539 Author chain B； PDBConstruct 1–498； UniProt 42–539

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1sjp
Deposition date deposition_date	2004-03-04
Structure title title	Mycobacterium tuberculosis Chaperonin60.2
Keywords keywords	CHAPERONE, Structural Genomics, PSI, Protein Structure Initiative, TB Structural Genomics Consortium, TBSGC; CHAPERONE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

1sjp__assembly_1__model_1

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

Download this curve (.dat)

1sjp__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1sjp__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	35.44 Å
Rg (electron density)	35.38 Å
Total Rg	35.60 Å
Atom count	6595
Residues	892
Excluded volume	118340 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1sjp__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (1)

▼

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1sjpa1
Class class	a — All alpha proteins
Fold Fold fold	a.129 — GroEL equatorial domain-like
Superfamily Superfamily superfamily	a.129.1 — GroEL equatorial domain-like
Family Family family	a.129.1.1 — GroEL chaperone, ATPase domain

Domain ID domain_id	d1sjpa2
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	d1sjpa3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.56 — GroEL-intermediate domain like
Superfamily Superfamily superfamily	d.56.1 — GroEL-intermediate domain like
Family Family family	d.56.1.1 — GroEL-like chaperone, intermediate domain

Domain ID domain_id	d1sjpb1
Class class	a — All alpha proteins
Fold Fold fold	a.129 — GroEL equatorial domain-like
Superfamily Superfamily superfamily	a.129.1 — GroEL equatorial domain-like
Family Family family	a.129.1.1 — GroEL chaperone, ATPase domain

Domain ID domain_id	d1sjpb2
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	d1sjpb3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.56 — GroEL-intermediate domain like
Superfamily Superfamily superfamily	d.56.1 — GroEL-intermediate domain like
Family Family family	d.56.1.1 — GroEL-like chaperone, intermediate domain

CATH v4.4 (6 domains)

Domain ID domain_id	1sjpA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	560 — GROEL; domain 1
Homologous superfamily homologous superfamily	10 — GroEL-like equatorial domain

Domain ID domain_id	1sjpA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	260 — GROEL; domain 2
Homologous superfamily homologous superfamily	10 — TCP-1-like chaperonin intermediate domain

Domain ID domain_id	1sjpA03
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	1sjpB01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	560 — GROEL; domain 1
Homologous superfamily homologous superfamily	10 — GroEL-like equatorial domain

Domain ID domain_id	1sjpB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	260 — GROEL; domain 2
Homologous superfamily homologous superfamily	10 — TCP-1-like chaperonin intermediate domain

Domain ID domain_id	1sjpB03
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	7 — GroEL
Homologous superfamily homologous superfamily	10 — GroEL

▶

Unit-cell length a length_a	58.674 Å
Unit-cell length b length_b	113.825 Å
Unit-cell length c length_c	79.535 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	94.58 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	3.200 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2436
R_work r_work	0.2414
R_free r_free	0.2849

Description description	60 kDa chaperonin 2
Molecular weight formula_weight	53049.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	6595

Mycobacterium tuberculosis Chaperonin60.2

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

60 kDa chaperonin 2

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

1sjp__assembly_1__model_1

1sjp__assembly_1__model_1 | I(q)

1sjp__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (2)

Source organism organism	Mycobacterium tuberculosis
NCBI taxonomy ID ncbi_taxonomy_id	1773
Host organism host_organism	Escherichia coli BL21(DE3)

Mycobacterium tuberculosis Chaperonin60.2

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

60 kDa chaperonin 2

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

1sjp__assembly_1__model_1

1sjp__assembly_1__model_1 | I(q)

1sjp__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (2)