SAXSdb — 2car

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

INOSINE TRIPHOSPHATE PYROPHOSPHATASE

HOMO SAPIENS

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ITPA_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–196； UniProt 1–194 Author chain B； PDBConstruct 3–196； UniProt 1–194

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	2car
Deposition date deposition_date	2005-12-22
Structure title title	Crystal Structure Of Human Inosine Triphosphatase
Keywords keywords	;HYDROLASE, INOSINE TRIPHOSPHATE PYROPHOSPHOHYDROLASE, INOSINE TRIPHOSPHATASE DEFICIENCY, ITP, IMP, DISEASE MUTATION, NUCLEOTIDE METABOLISM ;; HYDROLASE
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.

2car__assembly_1__model_1

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

Download this curve (.dat)

2car__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2car__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	24.66 Å
Rg (electron density)	23.74 Å
Total Rg	24.61 Å
Atom count	3028
Residues	390
Excluded volume	54202 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2car__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 (2)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2cara1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.51 — Anticodon-binding domain-like
Superfamily Superfamily superfamily	c.51.4 — ITPase-like
Family Family family	c.51.4.1 — ITPase (Ham1)

Domain ID domain_id	d2carb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.51 — Anticodon-binding domain-like
Superfamily Superfamily superfamily	c.51.4 — ITPase-like
Family Family family	c.51.4.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id	2carA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	950 — Maf protein
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2carB00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	950 — Maf protein
Homologous superfamily homologous superfamily	10 —

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Unit-cell length a length_a	31.230 Å
Unit-cell length b length_b	105.000 Å
Unit-cell length c length_c	50.140 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.01 °
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	1.090 Å
Low-resolution limit resolution_low	40.000 Å
R factor r_factor	0.0954
R_work r_work	—
R_free r_free	0.1534

Description description	INOSINE TRIPHOSPHATE PYROPHOSPHATASE
Molecular weight formula_weight	21612.8 kDa
EC 编号 ec_number	3.6.1.19
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	3905

Crystal Structure Of Human Inosine Triphosphatase

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

INOSINE TRIPHOSPHATE PYROPHOSPHATASE

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

2car__assembly_1__model_1

2car__assembly_1__model_1 | I(q)

2car__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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
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	648

Crystal Structure Of Human Inosine Triphosphatase

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

INOSINE TRIPHOSPHATE PYROPHOSPHATASE

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

2car__assembly_1__model_1

2car__assembly_1__model_1 | I(q)

2car__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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)