SAXSdb — 4g39

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

Sulfite reductase [NADPH] hemoprotein beta-component

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	PHOSPHATE ION × 1 POTASSIUM ION × 2 IRON/SULFUR CLUSTER × 1 SIROHEME × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CYSI_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 81–570； UniProt 81–570

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	4g39
Deposition date deposition_date	2012-07-13
Structure title title	Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer
Keywords keywords	SNiRR, oxidoreductase, sulfite reductase flavoprotein; 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.

4g39__assembly_1__model_1

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

Download this curve (.dat)

4g39__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4g39__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.36 Å
Rg (electron density)	21.54 Å
Total Rg	22.30 Å
Atom count	3730
Residues	465
Excluded volume	66570 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4g39__assembly_1__model_1`	monomeric （1）	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 (6)

Entity 1 Entity 1 polymer

Description description	Sulfite reductase [NADPH] hemoprotein beta-component
Molecular weight formula_weight	64021.0 kDa
EC 编号 ec_number	1.8.1.2
Mutation mutation	R153S
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	3875

MSEKHPGPLVVEGKLTDAERMKHESNYLRGTIAEDLNDGLTGGFKGDNFLLIRFHGMYQQDDRDIRAERAEQKLEPRHAMLLRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNSNVLCTSNPYESQLHAEAYEWAKKISEHLLPRTRAYAEIWLDQEKVATTDEEPILGQTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGGGLSIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVETFKAEVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDNWHLTLFIENGRILDYPARPLKTGLLEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKIAKESGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAKHGVSDEHIVMRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGIIRPVLDPARDLWD

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	83333
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 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 non-polymer

Description description	SIROHEME
Molecular weight formula_weight	916.7 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	117

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6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d4g39a1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.36 — Nitrite/Sulfite reductase N-terminal domain-like
Family Family family	d.58.36.0 — automated matches

Domain ID domain_id	d4g39a2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.134 — Nitrite and sulphite reductase 4Fe-4S domain-like
Superfamily Superfamily superfamily	d.134.1 — Nitrite and sulphite reductase 4Fe-4S domain-like
Family Family family	d.134.1.0 — automated matches

Domain ID domain_id	d4g39a3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.36 — Nitrite/Sulfite reductase N-terminal domain-like
Family Family family	d.58.36.0 — automated matches

Domain ID domain_id	d4g39a4
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.134 — Nitrite and sulphite reductase 4Fe-4S domain-like
Superfamily Superfamily superfamily	d.134.1 — Nitrite and sulphite reductase 4Fe-4S domain-like
Family Family family	d.134.1.0 — automated matches

CATH v4.4 (3 domains)

Domain ID domain_id	4g39A01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	480 — Sulfite Reductase Hemoprotein; domain 2
Homologous superfamily homologous superfamily	10 — Sulfite Reductase Hemoprotein;Domain 2

Domain ID domain_id	4g39A02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	413 — Sulfite Reductase Hemoprotein; domain 1
Homologous superfamily homologous superfamily	10 — Sulfite Reductase Hemoprotein, domain 1

Domain ID domain_id	4g39A03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	413 — Sulfite Reductase Hemoprotein; domain 1
Homologous superfamily homologous superfamily	10 — Sulfite Reductase Hemoprotein, domain 1

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Unit-cell length a length_a	67.598 Å
Unit-cell length b length_b	77.045 Å
Unit-cell length c length_c	86.851 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1782
R_work r_work	0.1726
R_free r_free	0.2375

Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer

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

Sulfite reductase [NADPH] hemoprotein beta-component

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

4g39__assembly_1__model_1

4g39__assembly_1__model_1 | I(q)

4g39__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 (6)

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 water

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (4 domains)

CATH v4.4 (3 domains)

7. Citations (1)

Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer

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

Sulfite reductase [NADPH] hemoprotein beta-component

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

4g39__assembly_1__model_1

4g39__assembly_1__model_1 | I(q)

4g39__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 (6)

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 water

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (4 domains)

CATH v4.4 (3 domains)

7. Citations (1)