SAXSdb — 2pvd

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

Ferredoxin-thioredoxin reductase, catalytic chain

Synechocystis sp.

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Ferredoxin-thioredoxin reductase, variable chain × 1 （Q55781） SULFATE ION × 1 IRON/SULFUR CLUSTER × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q55389_SYNY3
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–107； UniProt 12–118

Ferredoxin-thioredoxin reductase, variable chain

Synechocystis sp.

UniProt Q55781

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Ferredoxin-thioredoxin reductase, catalytic chain × 1 （Q55389） SULFATE ION × 1 IRON/SULFUR CLUSTER × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FTRV_SYNY3
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–73； UniProt 1–73

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	2pvd
Deposition date deposition_date	2007-05-09
Structure title title	Crystal srtucture of the reduced ferredoxin:thioredoxin reductase
Keywords keywords	Thioredoxin, redox, iron-sulfur, ELECTRON TRANSPORT; ELECTRON TRANSPORT
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.

2pvd__assembly_1__model_1

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

Download this curve (.dat)

2pvd__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2pvd__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.08 Å
Rg (electron density)	17.39 Å
Total Rg	18.02 Å
Atom count	1432
Residues	180
Excluded volume	25451 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2pvd__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 (5)

Entity 1 Entity 1 polymer

Description description	Ferredoxin-thioredoxin reductase, catalytic chain
Molecular weight formula_weight	12110.9 kDa
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	1509

LAAMKNFAEQYAKRTDTYFCSDLSVTAVVIEGLARHKEELGSPLCPCRHYADKEAEVKNTFWNCPCVPMRERKECHCMLFLTPDNDFAGDAQGIPMETLEEKKASMA

Source Source

Source organism organism	Synechocystis sp.
NCBI taxonomy ID ncbi_taxonomy_id	1143
Host organism host_organism	Escherichia coli BL21

Entity 2 Entity 2 polymer

Description description	Ferredoxin-thioredoxin reductase, variable chain
Molecular weight formula_weight	8196.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MNVGDRVRVTSSVVVYHHPEHAKTAFDLQGMEGEVAAVLTGWQGRPISANLPVLVKFEQRFKAHFRPDEVTLI

Source Source

Source organism organism	Synechocystis sp.
NCBI taxonomy ID ncbi_taxonomy_id	1143
Host organism host_organism	Escherichia coli BL21

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	IRON/SULFUR CLUSTER
Molecular weight formula_weight	351.6 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	77

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2pvda_
Class class	g — Small proteins
Fold Fold fold	g.36 — Ferredoxin thioredoxin reductase (FTR), catalytic beta chain
Superfamily Superfamily superfamily	g.36.1 — Ferredoxin thioredoxin reductase (FTR), catalytic beta chain
Family Family family	g.36.1.1 — Ferredoxin thioredoxin reductase (FTR), catalytic beta chain

Domain ID domain_id	d2pvdb_
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.4 — Electron transport accessory proteins
Family Family family	b.34.4.3 — Ferredoxin thioredoxin reductase (FTR), alpha (variable) chain

CATH v4.4 (2 domains)

Domain ID domain_id	2pvdA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	460 — Ferredoxin Thioredoxin Reductase
Homologous superfamily homologous superfamily	10 — Ferredoxin thioredoxin reductase catalytic beta subunit

Domain ID domain_id	2pvdB00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	50 —

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Unit-cell length a length_a	45.177 Å
Unit-cell length b length_b	45.177 Å
Unit-cell length c length_c	172.730 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	1.950 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.2680
R_free r_free	0.2840

Crystal srtucture of the reduced ferredoxin:thioredoxin reductase

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

Ferredoxin-thioredoxin reductase, catalytic chain

State in the Current Structure

Other States of the Same Protein in the Database

Ferredoxin-thioredoxin reductase, variable chain

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

2pvd__assembly_1__model_1

2pvd__assembly_1__model_1 | I(q)

2pvd__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Crystal srtucture of the reduced ferredoxin:thioredoxin reductase

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

Ferredoxin-thioredoxin reductase, catalytic chain

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Ferredoxin-thioredoxin reductase, variable chain

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

2pvd__assembly_1__model_1

2pvd__assembly_1__model_1 | I(q)

2pvd__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)