SAXSdb — 3fwy

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

Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein

Rhodobacter sphaeroides 2.4.1

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	MAGNESIUM ION × 2 ADENOSINE-5'-DIPHOSPHATE × 2 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	BCHL_RHOS4
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 19–314； UniProt 2–297 Author chain B； PDBConstruct 19–314； UniProt 2–297

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	3fwy
Deposition date deposition_date	2009-01-19
Structure title title	Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase (BchL) with MgADP bound: a homologue of the nitrogenase Fe protein
Keywords keywords	;BchL, protochlorophyllide, Electron donor, DPOR, Fe protein, nitrogenase, mixed alpha-beta domain, MgADP, ATP-binding, Bacteriochlorophyll biosynthesis, Chlorophyll biosynthesis, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, Oxidoreductase, Photosynthesis ;; 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.

3fwy__assembly_1__model_1

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

Download this curve (.dat)

3fwy__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3fwy__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	24.14 Å
Rg (electron density)	23.15 Å
Total Rg	23.84 Å
Atom count	4176
Residues	536
Excluded volume	74052 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3fwy__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	Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Molecular weight formula_weight	34515.0 kDa
EC 编号 ec_number	1.18.-.-
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4630

MHHHHHHHGMHHHHHHHGSPKDLTIPTGADGEGSVQVHLDEADKITGAKVFAVYGKGGIGKSTTSSNLSAAFSILGKRVLQIGCDPKHDSTFTLTGSLVPTVIDVLKDVDFHPEELRPEDFVFEGFNGVMCVEAGGPPAGTGCGGYVVGQTVKLLKQHHLLDDTDVVIFDVLGDVVCGGFAAPLQHADQAVVVTANDFDSIYAMNRIIAAVQAKSKNYKVRLAGCVANRSRATDEVDRFCKETNFRRLAHMPDLDAIRRSRLKKKTLFEMDEDQDVLAARAEYIRLAESLWRGLDPIDPHSLPDRDIFELLGFD

Source Source

Source organism organism	Rhodobacter sphaeroides 2.4.1
NCBI taxonomy ID ncbi_taxonomy_id	272943
Host organism host_organism	Azotobacter vinelandii

Entity 2 Entity 2 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	2

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	402

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d3fwya_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.0 — automated matches

Domain ID domain_id	d3fwyb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id	3fwyA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	3fwyB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

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Unit-cell length a length_a	56.729 Å
Unit-cell length b length_b	86.622 Å
Unit-cell length c length_c	117.169 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 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.630 Å
Low-resolution limit resolution_low	33.020 Å
R factor r_factor	0.1753
R_work r_work	0.1740
R_free r_free	0.1986

Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase (BchL) with MgADP bound: a homologue of the nitrogenase Fe protein

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

Light-independent protochlorophyllide reductase iron-sulfur ATP-binding 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

3fwy__assembly_1__model_1

3fwy__assembly_1__model_1 | I(q)

3fwy__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 non-polymer

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 structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase (BchL) with MgADP bound: a homologue of the nitrogenase Fe protein

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

Light-independent protochlorophyllide reductase iron-sulfur ATP-binding 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

3fwy__assembly_1__model_1

3fwy__assembly_1__model_1 | I(q)

3fwy__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 non-polymer

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)