SAXSdb — 2a0m

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

ARGINASE SUPERFAMILY PROTEIN

Trypanosoma cruzi

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	CHLORIDE ION × 1 water × 1	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 3	CHLORIDE ION × 3 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q4DSA0_TRYCR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 9–316； UniProt 1–308

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	2a0m
Deposition date deposition_date	2005-06-16
Structure title title	Arginase superfamily protein from Trypanosoma cruzi
Keywords keywords	;STRUCTURAL GENOMICS, ARGINASE, PSI, Protein Structure Initiative, Structural Genomics of Pathogenic Protozoa Consortium, SGPP, HYDROLASE ;; 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.

2a0m__assembly_1__model_1

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

Download this curve (.dat)

2a0m__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2a0m__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.93 Å
Rg (electron density)	17.69 Å
Total Rg	18.68 Å
Atom count	2287
Residues	298
Excluded volume	40426 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2a0m__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2a0m__assembly_2__model_1`	trimeric （3）	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	ARGINASE SUPERFAMILY PROTEIN
Molecular weight formula_weight	34678.3 kDa
EC 编号 ec_number	3.5.3.8
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2500

MAHHHHHHMAARTDDPRLLSLFSAQREEDADIVIIGFPYDEGCVRNGGRAGAKKGPAAFRFFLQRLGSVNNLELNVDASHLKLYDAGDITASTLEEAHEKLESKVFTVLARGAFPFVIGGGNDQSAPNGRAMLRAFPGDVGVINVDSHLDVRPPLQDGRVHSGTPFRQLLEESSFSGKRFVEFACQGSQCGALHAQYVRDHQGHLMWLSEVRKKGAVAALEDAFGLTGKNTFFSFDVDSLKSSDMPGVSCPAAVGLSAQEAFDMCFLAGKTPTVMMMDMSELNPLVEEYRSPRVAVYMFYHFVLGFATRPKPKAEN

Source Source

Source organism organism	Trypanosoma cruzi
NCBI taxonomy ID ncbi_taxonomy_id	5693
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 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	202

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2a0ma1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.42 — Arginase/deacetylase
Superfamily Superfamily superfamily	c.42.1 — Arginase/deacetylase
Family Family family	c.42.1.1 — Arginase-like amidino hydrolases

CATH v4.4 (1 domains)

Domain ID domain_id	2a0mA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	800 — Arginase; Chain A
Homologous superfamily homologous superfamily	10 — Ureohydrolase domain

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Unit-cell length a length_a	128.875 Å
Unit-cell length b length_b	128.875 Å
Unit-cell length c length_c	42.671 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	9

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	—

Resolution resolution	1.603 Å
Low-resolution limit resolution_low	39.873 Å
R factor r_factor	—
R_work r_work	0.1680
R_free r_free	0.1954

Arginase superfamily protein from Trypanosoma cruzi

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

ARGINASE SUPERFAMILY PROTEIN

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

2a0m__assembly_1__model_1

2a0m__assembly_1__model_1 | I(q)

2a0m__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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

Arginase superfamily protein from Trypanosoma cruzi

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

ARGINASE SUPERFAMILY PROTEIN

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

2a0m__assembly_1__model_1

2a0m__assembly_1__model_1 | I(q)

2a0m__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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)