SAXSdb — 2pvo

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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 4	Ferredoxin-thioredoxin reductase, variable chain × 1 （Q55781） Thioredoxin F-type, chloroplast × 1 （P09856） Ferredoxin-1 × 1 （P27320） SULFATE ION × 2 IRON/SULFUR CLUSTER × 1 FE2/S2 (INORGANIC) CLUSTER × 1	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 1–110； UniProt 9–118

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 4	Ferredoxin-thioredoxin reductase, catalytic chain × 1 （Q55389） Thioredoxin F-type, chloroplast × 1 （P09856） Ferredoxin-1 × 1 （P27320） SULFATE ION × 2 IRON/SULFUR CLUSTER × 1 FE2/S2 (INORGANIC) CLUSTER × 1	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 1–74； UniProt 1–74

Thioredoxin F-type, chloroplast

Spinacia oleracea

UniProt P09856

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Ferredoxin-thioredoxin reductase, catalytic chain × 1 （Q55389） Ferredoxin-thioredoxin reductase, variable chain × 1 （Q55781） Ferredoxin-1 × 1 （P27320） SULFATE ION × 2 IRON/SULFUR CLUSTER × 1 FE2/S2 (INORGANIC) CLUSTER × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TRXF_SPIOL
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–111； UniProt 79–189

Ferredoxin-1

Synechocystis sp.

UniProt P27320

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Ferredoxin-thioredoxin reductase, catalytic chain × 1 （Q55389） Ferredoxin-thioredoxin reductase, variable chain × 1 （Q55781） Thioredoxin F-type, chloroplast × 1 （P09856） SULFATE ION × 2 IRON/SULFUR CLUSTER × 1 FE2/S2 (INORGANIC) CLUSTER × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FER_SYNY3
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain D； PDBConstruct 1–96； UniProt 2–97

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	2pvo
Deposition date deposition_date	2007-05-09
Structure title title	Crystal srtucture of the ternary complex between thioredoxin f, ferredoxin, and ferredoxin: thioredoxin reductase
Keywords keywords	Thioredoxin, ferredoxin. redox, iron-sulfur cluster, protein-protein complex, 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.

2pvo__assembly_1__model_1

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

Download this curve (.dat)

2pvo__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2pvo__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	23.43 Å
Rg (electron density)	22.84 Å
Total Rg	23.41 Å
Atom count	3071
Residues	391
Excluded volume	54682 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2pvo__assembly_1__model_1`	tetrameric （4）	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 (7)

Entity 1 Entity 1 polymer

Description description	Ferredoxin-thioredoxin reductase, catalytic chain
Molecular weight formula_weight	12541.3 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	3071

NKTLAAMKNFAEQYAKRTDTYFCSDLSVTAVVIEGLARHKEELGSPLCPCRHYEDKEAEVKNTFWNCPCVPMRERKECHCMLFLTPDNDFAGDAQDIPMETLEEVKASMA

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	8455.7 kDa
Mutation mutation	C49S
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MNVGDRVRVTSSVVVYHHPEHKKTAFDLQGMEGEVAAVLTEWQGRPISANLPVLVKFEQRFKAHFRPDEVTLIE

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 polymer

Description description	Thioredoxin F-type, chloroplast
Molecular weight formula_weight	12360.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

EAIVGKVTEVNKDTFWPIVKAAGDKPVVLDMFTQWCGPSKAMAPKYEKLAEEYLDVIFLKLDCNQENKTLAKELGIRVVPTFKILKENSVVGEVTGAKYDKLLEAIQAARS

Source Source

Source organism organism	Spinacia oleracea
Common name common_name	spinach
NCBI taxonomy ID ncbi_taxonomy_id	3562
Host organism host_organism	Escherichia coli BL21

Entity 4 Entity 4 polymer

Description description	Ferredoxin-1
Molecular weight formula_weight	10251.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

ASYTVKLITPDGESSIECSDDTYILDAAEEAGLELPYSCRAGACSTCAGKITAGSVDQSDQSFLDDDQIEAGYVLTCVAYPTSDCTIETHKEEDLY

Source Source

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

Entity 5 Entity 5 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 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 7 Entity 7 non-polymer

Description description	FE2/S2 (INORGANIC) CLUSTER
Molecular weight formula_weight	175.8 kDa
Source method src_method	syn
Copy count entity_count	1

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2pvoa1
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	d2pvob1
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 (4 domains)

Domain ID domain_id	2pvoA00
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	2pvoB00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	2pvoC00
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	2pvoD00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	30 — Beta-grasp domain

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Unit-cell length a length_a	130.426 Å
Unit-cell length b length_b	130.426 Å
Unit-cell length c length_c	63.837 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	6

Space group space_group	P 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	3.400 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	—
R_work r_work	0.2020
R_free r_free	0.2630

Crystal srtucture of the ternary complex between thioredoxin f, ferredoxin, and 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

Thioredoxin F-type, chloroplast

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-1

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

2pvo__assembly_1__model_1

2pvo__assembly_1__model_1 | I(q)

2pvo__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)