4p3e

Structure of the human SRP S domain

Method: X-RAY DIFFRACTION Dmax: 117.1 Å Quality: REASONABLE

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

Signal recognition particle 19 kDa protein

Homo sapiens

UniProt P09132

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 2 RNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain B; UniProt 1–120 Fragment:UNP residues 1-120 SRP RNA (124-mer) × 1 Signal recognition particle subunit SRP68 × 1 (Q9UHB9) MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;291 K;Ammonium sulfate, Sodium malonate Resolution 3.50 Å R-free 0.285

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SRP19_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–120; UniProt 1–120

Signal recognition particle subunit SRP68

Homo sapiens

UniProt Q9UHB9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 2 RNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain C; UniProt 47–254 Fragment:UNP residues 47-254 Mutation:E108D SRP RNA (124-mer) × 1 Signal recognition particle 19 kDa protein × 1 (P09132) MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;291 K;Ammonium sulfate, Sodium malonate Resolution 3.50 Å R-free 0.285

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SRP68_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 9–216; UniProt 47–254

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.

SAXS scattering curve SAXS Profile

SAXS profile for 4p3e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4p3e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4p3e
Deposition date deposition_date2014-03-07
Structure title titleStructure of the human SRP S domain
Keywords keywordsSRP, SRP RNA, SRP19, SRP68, ribonucleoprotein particle (RNP), Arginine-rich motif (ARM), RNA BINDING PROTEIN-RNA complex; RNA BINDING PROTEIN/RNA
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier33.98
Radius of gyration Rg (electron density) rg_electron35.78
Forward intensity I(0) i0167410000.00
Molecular weight molecular_weight73807.0 kDa
Excluded volume excluded_volume79296 ų
Envelope volume envelope_volume118420 ų
Hydration-shell volume shell_volume30077 ų
Envelope diameter envelope_diameter125.1
Shell Rg shell_rg38.41
Envelope Rg envelope_rg35.59
Shape Rg shape_rg35.83
Total Rg total_rg35.81
Total atoms total_atoms5011
Residues n_residues408
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax117.1
Rg (real space) rg_real34.35
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real1.6740e+08
I(0) uncertainty (real space) i0_real_error2.7250e+06
Rg (reciprocal space) rg_reciprocal34.12
I(0) (reciprocal space) i0_reciprocal167400000.0000
Solution quality estimate total_estimate0.6083
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.573
Kurtosis Kurtosis kurtosis-0.391
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9746000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.663; Stabil: 1.000; Sysdev: 0.214; Positv: 1.000; Valcen: 0.486; Smooth: 0.786

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4p3eB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology56 — Phenylalanyl-tRNA Synthetase; Chain B, domain 1
Homologous superfamily homologous superfamily30 — Signal recognition particle, SRP19-like subunit
Domain ID domain_id4p3eC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology3450 — Hyaluronidase domain-like
Homologous superfamily homologous superfamily40 — Signal recognition particle, SRP68 subunit, RNA-binding domain

8. Citations (1)

9. Files and Curves (10)