SAXSdb — 1e8s

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

SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN

HOMO SAPIENS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–RNA	Heteromer	Protein 2 RNA 1	SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN × 1 （P37108） 7SL RNA, 88-MER × 1 EUROPIUM (III) ION × 2	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SR09_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–85； UniProt 1–85

SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN

HOMO SAPIENS

UniProt P37108

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–RNA	Heteromer	Protein 2 RNA 1	SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN × 1 （P49458） 7SL RNA, 88-MER × 1 EUROPIUM (III) ION × 2	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SR14_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–106； UniProt 2–107

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	1e8s
Deposition date deposition_date	2000-09-29
Structure title title	Alu domain of the mammalian SRP (potential Alu retroposition intermediate)
Keywords keywords	ALU RIBONUCLEOPROTEIN PARTICLE, ALU RNP ASSEMBLY AND DIMERISATION, TRANSLATIONAL CONTROL, ALU RETROPOSITION; ALU RIBONUCLEOPROTEIN PARTICLE
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.

1e8s__assembly_1__model_1

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

Download this curve (.dat)

1e8s__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1e8s__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	27.66 Å
Rg (electron density)	22.99 Å
Total Rg	23.25 Å
Atom count	88
Residues	86
Excluded volume	21459 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1e8s__assembly_1__model_1`	trimeric （3）	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 (4)

Entity 1 Entity 1 polymer

Description description	SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN
Molecular weight formula_weight	9996.6 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	235

PQYQTWEEFSRAAEKLYLADPMKARVVLKYRHSDGNLCVKVTDDLVCLVYKTDQAQDVKKIEKFHSQLMRLMVAKEARNVTMETE

Source Source

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN
Molecular weight formula_weight	12114.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

VLLESEQFLTELTRLFQKCRTSGSVYITLKKYDGRTKPIPKKGTVEGFEPADNKCLLRATDGKKKISTVVSSKEVNKFQMAYSNLLRANMDGLKKRDKKNKTKKTK

Source Source

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 polymer

Description description	7SL RNA, 88-MER
Molecular weight formula_weight	28490.9 kDa
Mutation mutation	YES
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polyribonucleotide
Chain IDs strand_id	C

GCUAGCGAGACCCCGUCUCUGCCGGGCGCGGUGGCGCGCGCCUGUAGUCCCAGCUACUCGGGAGGCUGAGGUGGGAGGAUCGCUAGUC

Entity 4 Entity 4 non-polymer

Description description	EUROPIUM (III) ION
Molecular weight formula_weight	152.0 kDa
Source method src_method	syn
Copy count entity_count	2

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1e8sa_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.49 — Signal recognition particle alu RNA binding heterodimer, SRP9/14
Superfamily Superfamily superfamily	d.49.1 — Signal recognition particle alu RNA binding heterodimer, SRP9/14
Family Family family	d.49.1.1 — Signal recognition particle alu RNA binding heterodimer, SRP9/14

Domain ID domain_id	d1e8sb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.49 — Signal recognition particle alu RNA binding heterodimer, SRP9/14
Superfamily Superfamily superfamily	d.49.1 — Signal recognition particle alu RNA binding heterodimer, SRP9/14
Family Family family	d.49.1.1 — Signal recognition particle alu RNA binding heterodimer, SRP9/14

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Unit-cell length a length_a	143.330 Å
Unit-cell length b length_b	143.330 Å
Unit-cell length c length_c	60.360 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 42 21 2
Space-group number int_tables_number	94
Crystal system crystal_system	—

Resolution resolution	4.000 Å
Low-resolution limit resolution_low	37.460 Å
R factor r_factor	0.3880
R_work r_work	0.3880
R_free r_free	—

Alu domain of the mammalian SRP (potential Alu retroposition intermediate)

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

SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

SIGNAL RECOGNITION PARTICLE 14 KDA 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

1e8s__assembly_1__model_1

1e8s__assembly_1__model_1 | I(q)

1e8s__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 (4)

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

Entity 4 Entity 4 non-polymer

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

7. Citations (1)

Alu domain of the mammalian SRP (potential Alu retroposition intermediate)

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

SIGNAL RECOGNITION PARTICLE 9 KDA 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

SIGNAL RECOGNITION PARTICLE 14 KDA 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

1e8s__assembly_1__model_1

1e8s__assembly_1__model_1 | I(q)

1e8s__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 (4)

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

Entity 4 Entity 4 non-polymer

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

7. Citations (1)