SAXSdb — 2v5b

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

TRIOSEPHOSPHATE ISOMERASE

TRYPANOSOMA CRUZI

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
2	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	TPIS_TRYCR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–68； UniProt 1–68 Author chain A； PDBConstruct 77–244； UniProt 84–251

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	2v5b
Deposition date deposition_date	2008-10-02
Structure title title	The monomerization of Triosephosphate Isomerase from Trypanosoma cruzi
Keywords keywords	;TIM, UNFOLDING, MONOTCTIM, ISOMERASE, GLYCOSOME, GLUCONEOGENESIS, LIPID SYNTHESIS, MONOMERIC MUTANT, GLYCOLYSIS, PENTOSE SHUNT, MONOMERIZATION, FATTY ACID BIOSYNTHESIS, TRIOSEPHOSPHATE 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.

2v5b__assembly_2__model_1

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

Download this curve (.dat)

2v5b__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2v5b__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	17.95 Å
Rg (electron density)	16.70 Å
Total Rg	17.75 Å
Atom count	1809
Residues	236
Excluded volume	32365 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2v5b__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2v5b__assembly_2__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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2v5ba_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.1 — Triosephosphate isomerase (TIM)
Family Family family	c.1.1.1 — Triosephosphate isomerase (TIM)

CATH v4.4 (1 domains)

Domain ID domain_id	2v5bA00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

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Unit-cell length a length_a	70.327 Å
Unit-cell length b length_b	77.673 Å
Unit-cell length c length_c	43.052 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	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	52.130 Å
R factor r_factor	0.2137
R_work r_work	0.2116
R_free r_free	0.2569

Description description	TRIOSEPHOSPHATE ISOMERASE
Molecular weight formula_weight	26514.4 kDa
EC 编号 ec_number	5.3.1.1
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1881

The monomerization of Triosephosphate Isomerase from Trypanosoma cruzi

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

TRIOSEPHOSPHATE ISOMERASE

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

2v5b__assembly_2__model_1

2v5b__assembly_2__model_1 | I(q)

2v5b__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

Source organism organism	TRYPANOSOMA CRUZI
NCBI taxonomy ID ncbi_taxonomy_id	5693
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	54

The monomerization of Triosephosphate Isomerase from Trypanosoma cruzi

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

TRIOSEPHOSPHATE ISOMERASE

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

2v5b__assembly_2__model_1

2v5b__assembly_2__model_1 | I(q)

2v5b__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)