SAXSdb — 3e0m

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

Peptide methionine sulfoxide reductase msrA/msrB 1

Streptococcus pneumoniae

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 7	Short peptide SHMAEI × 3 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MSAB1_STRPN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–313； UniProt 1–312 Author chain B； PDBConstruct 2–313； UniProt 1–312 Author chain C； PDBConstruct 2–313； UniProt 1–312 Author chain D； PDBConstruct 2–313； UniProt 1–312

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	3e0m
Deposition date deposition_date	2008-07-31
Structure title title	Crystal structure of fusion protein of MsrA and MsrB
Keywords keywords	fusion, MsrAB, linker, hinge, Cell membrane, Membrane, Multifunctional enzyme, Oxidoreductase; 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.

3e0m__assembly_1__model_1

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

Download this curve (.dat)

3e0m__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3e0m__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	37.02 Å
Rg (electron density)	36.45 Å
Total Rg	36.93 Å
Atom count	10209
Residues	1264
Excluded volume	179990 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3e0m__assembly_1__model_1`	heptameric （7）	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 (3)

Entity 1 Entity 1 polymer

Description description	Peptide methionine sulfoxide reductase msrA/msrB 1
Molecular weight formula_weight	35881.0 kDa
EC 编号 ec_number	1.8.4.11, 1.8.4.12
Mutation mutation	I238L
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	10514

HMAEIYLAGGCFWGLEEYFSRISGVLETSVGYANGQVETTNYQLLKETDHAETVQVIYDEKEVSLREILLYYFRVIDPLSINQQGNDRGRQYRTGIYYQDEADLPAIYTVVQEQERMLGRKIAVEVEQLRHYILAEDYHQDYLRKNPSGYCHIDVTDADKPLIDAANYEKPSQEVLKASLSEESYRVTQEAATEAPFTNAYDQTFEEGIYVDITTGEPLFFAKDKFASGCGWPSFSRPLSKELIHYYKDLSHGMERIEVRSRSGSAHLGHVFTDGPRELGGLRYCINSASLRFVAKDEMEKAGYGYLLPYLNK

Source Source

Source organism organism	Streptococcus pneumoniae
NCBI taxonomy ID ncbi_taxonomy_id	1313
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Short peptide SHMAEI
Molecular weight formula_weight	687.8 kDa
Source method src_method	syn
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G

SHMAEI

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	305

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6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id	3e0mA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1060 — Peptide Methionine Sulfoxide Reductase; Chain A
Homologous superfamily homologous superfamily	10 — Peptide methionine sulphoxide reductase MsrA

Domain ID domain_id	3e0mA02
Class class	2 — Mainly Beta
Architecture architecture	170 — Beta Complex
Topology topology	150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily	20 — Peptide methionine sulfoxide reductase.

Domain ID domain_id	3e0mB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1060 — Peptide Methionine Sulfoxide Reductase; Chain A
Homologous superfamily homologous superfamily	10 — Peptide methionine sulphoxide reductase MsrA

Domain ID domain_id	3e0mB02
Class class	2 — Mainly Beta
Architecture architecture	170 — Beta Complex
Topology topology	150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily	20 — Peptide methionine sulfoxide reductase.

Domain ID domain_id	3e0mC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1060 — Peptide Methionine Sulfoxide Reductase; Chain A
Homologous superfamily homologous superfamily	10 — Peptide methionine sulphoxide reductase MsrA

Domain ID domain_id	3e0mC02
Class class	2 — Mainly Beta
Architecture architecture	170 — Beta Complex
Topology topology	150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily	20 — Peptide methionine sulfoxide reductase.

Domain ID domain_id	3e0mD01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1060 — Peptide Methionine Sulfoxide Reductase; Chain A
Homologous superfamily homologous superfamily	10 — Peptide methionine sulphoxide reductase MsrA

Domain ID domain_id	3e0mD02
Class class	2 — Mainly Beta
Architecture architecture	170 — Beta Complex
Topology topology	150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily	20 — Peptide methionine sulfoxide reductase.

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Unit-cell length a length_a	158.521 Å
Unit-cell length b length_b	165.489 Å
Unit-cell length c length_c	77.281 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	16

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	19.990 Å
R factor r_factor	0.2390
R_work r_work	0.2390
R_free r_free	0.2820

Crystal structure of fusion protein of MsrA and MsrB

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

Peptide methionine sulfoxide reductase msrA/msrB 1

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

3e0m__assembly_1__model_1

3e0m__assembly_1__model_1 | I(q)

3e0m__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)

Crystal structure of fusion protein of MsrA and MsrB

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

Peptide methionine sulfoxide reductase msrA/msrB 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

3e0m__assembly_1__model_1

3e0m__assembly_1__model_1 | I(q)

3e0m__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)