2x99

Thioredoxin glutathione reductase from Schistosoma mansoni in complex with NADPH

Method: X-RAY DIFFRACTION

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

THIOREDOXIN GLUTATHIONE REDUCTASE

SCHISTOSOMA MANSONI

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 NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 GLUTATHIONE × 4 CALCIUM ION × 2 DI(HYDROXYETHYL)ETHER × 12 TETRAETHYLENE GLYCOL × 10 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q962Y6_SCHMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–598； UniProt 1–598

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	2x99
Deposition date deposition_date	2010-03-15
Structure title title	Thioredoxin glutathione reductase from Schistosoma mansoni in complex with NADPH
Keywords keywords	FLAVOPROTEIN, OXIDOREDUCTASE, THIOREDOXIN, GLUTATHIONE, NADPH, DETOXIFICATION PATHWAY; OXIDOREDUCTASE
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.

2x99__assembly_1__model_1

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

Download this curve (.dat)

2x99__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2x99__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	34.31 Å
Rg (electron density)	33.92 Å
Total Rg	34.47 Å
Atom count	9490
Residues	1174
Excluded volume	169650 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2x99__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 (8)

Entity 1 Entity 1 polymer

Description description	THIOREDOXIN GLUTATHIONE REDUCTASE
Molecular weight formula_weight	65061.1 kDa
EC 编号 ec_number	1.6.4.5
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	4936

MPPADGTSQWLRKTVDSAAVILFSKTTCPYCKKVKDVLAEAKIKHATIELDQLSNGSAIQKCLASFSKIETVPQMFVRGKFIGDSQTVLKYYSNDELAGIVNESKYDYDLIVIGGGSGGLAAGKEAAKYGAKTAVLDYVEPTPIGTTWGLGGTCVNVGCIPKKLMHQAGLLSHALEDAEHFGWSLDRSKISHNWSTMVEGVQSHIGSLNWGYKVALRDNQVTYLNAKGRLISPHEVQITDKNQKVSTITGNKIILATGERPKYPEIPGAVEYGITSDDLFSLPYFPGKTLVIGASYVALECAGFLASLGGDVTVMVRSILLRGFDQQMAEKVGDYMENHGVKFAKLCVPDEIKQLKVVDTENNKPGLLLVKGHYTDGKKFEEEFETVIFAVGREPQLSKVLCETVGVKLDKNGRVVCTDDEQTTVSNVYAIGDINAGKPQLTPVAIQAGRYLARRLFAGATELTDYSNVATTVFTPLEYGACGLSEEDAIEKYGDKDIEVYHSNFKPLEWTVAHREDNVCYMKLVCRKSDNMRVLGLHVLGPNAGEITQGYAVAIKMGATKADFDRTIGIHPTCSETFTTLHVTKKSGVSPIVSGCCG

Source Source

Source organism organism	SCHISTOSOMA MANSONI
NCBI taxonomy ID ncbi_taxonomy_id	6183
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	1

Entity 3 Entity 3 non-polymer

Description description	NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
Molecular weight formula_weight	745.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	GLUTATHIONE
Molecular weight formula_weight	307.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	DI(HYDROXYETHYL)ETHER
Molecular weight formula_weight	106.1 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 7 Entity 7 non-polymer

Description description	TETRAETHYLENE GLYCOL
Molecular weight formula_weight	194.2 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 8 Entity 8 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	185

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	2x99A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	2x99A02
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2x99A03
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	2x99A04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	30 — FAD/NAD-linked reductase, C-terminal dimerisation domain

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Unit-cell length a length_a	141.502 Å
Unit-cell length b length_b	102.610 Å
Unit-cell length c length_c	59.938 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	112.82 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	40.000 Å
R factor r_factor	0.1918
R_work r_work	0.1897
R_free r_free	0.2312

Thioredoxin glutathione reductase from Schistosoma mansoni in complex with NADPH

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

THIOREDOXIN GLUTATHIONE 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

2x99__assembly_1__model_1

2x99__assembly_1__model_1 | I(q)

2x99__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 (8)

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 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (3)

Thioredoxin glutathione reductase from Schistosoma mansoni in complex with NADPH

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

THIOREDOXIN GLUTATHIONE 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

2x99__assembly_1__model_1

2x99__assembly_1__model_1 | I(q)

2x99__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 (8)

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 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (3)