SAXSdb — 2x1t

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

TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL

TRYPANOSOMA BRUCEI BRUCEI

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	4-PHOSPHO-D-ERYTHRONOHYDROXAMIC ACID × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TPIS_TRYBB
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–12； UniProt 2–13 Author chain A； PDBConstruct 13–70； UniProt 15–72 Author chain A； PDBConstruct 71–225； UniProt 80–234 Author chain A； PDBConstruct 226–238； UniProt 238–250 Author chain B； PDBConstruct 1–12； UniProt 2–13 Author chain B； PDBConstruct 13–70； UniProt 15–72 Author chain B； PDBConstruct 71–225； UniProt 80–234 Author chain B； PDBConstruct 226–238； UniProt 238–250

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	2x1t
Deposition date deposition_date	2010-01-04
Structure title title	Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase
Keywords keywords	FATTY ACID BIOSYNTHESIS, GLUCONEOGENESIS, GLYCOLYSIS, GLYCOSOME, ISOMERASE, LIPID SYNTHESIS; 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.

2x1t__assembly_1__model_1

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

Download this curve (.dat)

2x1t__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2x1t__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	17.92 Å
Rg (electron density)	16.65 Å
Total Rg	17.69 Å
Atom count	1778
Residues	233
Excluded volume	31819 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2x1t__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2x1t__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 (3)

Entity 1 Entity 1 polymer

Description description	TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL
Molecular weight formula_weight	25659.3 kDa
EC 编号 ec_number	5.3.1.1
Mutation mutation	YES
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	4209

SKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVASTFVHLAMTKERLSHPKFVIAAQNAGNADALASLKDFGVNWIVLGHSERRWYYGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRILYGGSVNGKNARTLYQQRDVNGFLAGLKPEFVDIIKATQ

Source Source

Source organism organism	TRYPANOSOMA BRUCEI BRUCEI
NCBI taxonomy ID ncbi_taxonomy_id	5702
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	4-PHOSPHO-D-ERYTHRONOHYDROXAMIC ACID
Molecular weight formula_weight	231.1 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	605

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2x1ta_
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)

Domain ID domain_id	d2x1tb_
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 (2 domains)

Domain ID domain_id	2x1tA00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	2x1tB00
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	45.640 Å
Unit-cell length b length_b	86.850 Å
Unit-cell length c length_c	55.880 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	97.33 °
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	1.830 Å
Low-resolution limit resolution_low	26.400 Å
R factor r_factor	0.1741
R_work r_work	0.1716
R_free r_free	0.2194

Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase

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

TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL

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

2x1t__assembly_1__model_1

2x1t__assembly_1__model_1 | I(q)

2x1t__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)

Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase

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

TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL

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

2x1t__assembly_1__model_1

2x1t__assembly_1__model_1 | I(q)

2x1t__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)