SAXSdb — 9ro3

▼

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

Thioredoxin reductase

Cryptosporidium parvum

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	FLAVIN-ADENINE DINUCLEOTIDE × 2 GOLD ION × 2 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	FLAVIN-ADENINE DINUCLEOTIDE × 2 GOLD ION × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	C8CCG0_CRYPV
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–521； UniProt 1–521 Author chain B； PDBConstruct 1–521； UniProt 1–521 Author chain C； PDBConstruct 1–521； UniProt 1–521 Author chain D； PDBConstruct 1–521； UniProt 1–521

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	9ro3
Deposition date deposition_date	2025-06-20
Structure title title	Crystal structure of Cryptosporidium parvum Thioredoxin Reductase in complex with the auranofin analogue AuP(OCH3)3Cl
Keywords keywords	reductase, FLAVOPROTEIN; FLAVOPROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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.

9ro3__assembly_1__model_1

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

Download this curve (.dat)

9ro3__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9ro3__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	30.89 Å
Rg (electron density)	30.27 Å
Total Rg	30.87 Å
Atom count	7572
Residues	983
Excluded volume	135250 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9ro3__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`9ro3__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Thioredoxin reductase
Molecular weight formula_weight	56300.4 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	15454

MKFTLVTILFLIFMKKAKIVMADLTFMYDLVVIGGGSGGMAAAKEAAKYGKKVALFDFVKPSTQGTKWGLGGTCVNVGCVPKKLMHYSALIASSIHHDAQMSGHKTSSSFEWGKLVETLRNHIRMLNFSYRTGLRVGNVEYINALAKLIDPHSVEYEDNGQKKTITSRYILLATGGRPSIPETVPGAIQYSITSDDIFFLSKSPGKTLVIGASYIGLETAGFLNELGFDTTVAMRSIPLRGFDRQCSEKIVEYMKATGTKFLVGVVPINIEKVNENIKVSFSDGSVEEFETVLYATGRNPDVKGLNLNAIGVEVSDSGKIIAPKDATSVPSIFAVGDIVEGRPELTPVAVKAGILLARRLFAGSNEFIDYDFVPTTVFTPIEYGHVGLSSEAAIAKYGEDDIEEYLSEFSTLEIAAAHREKPEHLRENEMDFALPLNCLAKLVVVKSQGEKVVGFHFVGPNAGEITQGFSLAVKLGATKKDFDDMIGIHPTDAEVFGILEVTKRSGESFVSSGGCGGGKCG

Source Source

Source organism organism	Cryptosporidium parvum
NCBI taxonomy ID ncbi_taxonomy_id	5807
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	GOLD ION
Molecular weight formula_weight	197.0 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	260

▶

Unit-cell length a length_a	74.296 Å
Unit-cell length b length_b	73.251 Å
Unit-cell length c length_c	189.519 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.59 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	45.500 Å
R factor r_factor	0.2060
R_work r_work	0.2042
R_free r_free	0.2414

Crystal structure of Cryptosporidium parvum Thioredoxin Reductase in complex with the auranofin analogue AuP(OCH3)3Cl

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

Thioredoxin reductase

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

9ro3__assembly_1__model_1

9ro3__assembly_1__model_1 | I(q)

9ro3__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Citations (1)

Crystal structure of Cryptosporidium parvum Thioredoxin Reductase in complex with the auranofin analogue AuP(OCH3)3Cl

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

Thioredoxin reductase

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

9ro3__assembly_1__model_1

9ro3__assembly_1__model_1 | I(q)

9ro3__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Citations (1)