SAXSdb — 2fp2

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

Chorismate mutase

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	8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O07746_MYCTU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–166； UniProt 34–199 Author chain B； PDBConstruct 1–166； UniProt 34–199

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	2fp2
Deposition date deposition_date	2006-01-15
Structure title title	Secreted Chorismate Mutase from Mycobacterium tuberculosis
Keywords keywords	alpha-helical, ISOMERASE; ISOMERASE
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.

2fp2__assembly_1__model_1

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

Download this curve (.dat)

2fp2__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2fp2__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	24.34 Å
Rg (electron density)	23.70 Å
Total Rg	24.41 Å
Atom count	2573
Residues	325
Excluded volume	45073 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2fp2__assembly_1__model_1`	dimeric （2）	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 (3)

Entity 1 Entity 1 polymer

Description description	Chorismate mutase
Molecular weight formula_weight	18495.5 kDa
EC 编号 ec_number	5.4.99.5
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3092

DGTSQLAELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEYSRFSDWKLNPASAPPEPPDLSASRSAIDSLNNRMLSQIWSHWSLLSAPSCAAQLDRAKRDIVRSRHLDSLYQRALTTATQSYCQALPPA

Source Source

Source organism organism	Mycobacterium tuberculosis
NCBI taxonomy ID ncbi_taxonomy_id	1773
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID
Molecular weight formula_weight	228.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	416

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2fp2a_
Class class	a — All alpha proteins
Fold Fold fold	a.130 — Chorismate mutase II
Superfamily Superfamily superfamily	a.130.1 — Chorismate mutase II
Family Family family	a.130.1.4 — Secreted chorismate mutase-like

Domain ID domain_id	d2fp2b_
Class class	a — All alpha proteins
Fold Fold fold	a.130 — Chorismate mutase II
Superfamily Superfamily superfamily	a.130.1 — Chorismate mutase II
Family Family family	a.130.1.4 — Secreted chorismate mutase-like

CATH v4.4 (2 domains)

Domain ID domain_id	2fp2A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	59 — Chorismate Mutase Domain, subunit A
Homologous superfamily homologous superfamily	10 — Chorismate mutase

Domain ID domain_id	2fp2B00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	59 — Chorismate Mutase Domain, subunit A
Homologous superfamily homologous superfamily	10 — Chorismate mutase

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Unit-cell length a length_a	42.906 Å
Unit-cell length b length_b	72.800 Å
Unit-cell length c length_c	61.716 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.99 °
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	1.640 Å
Low-resolution limit resolution_low	38.920 Å
R factor r_factor	0.1718
R_work r_work	0.1702
R_free r_free	0.2033

Secreted Chorismate Mutase from Mycobacterium tuberculosis

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

Chorismate mutase

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

2fp2__assembly_1__model_1

2fp2__assembly_1__model_1 | I(q)

2fp2__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Secreted Chorismate Mutase from Mycobacterium tuberculosis

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

Chorismate mutase

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

2fp2__assembly_1__model_1

2fp2__assembly_1__model_1 | I(q)

2fp2__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)