5m73

Structure of the human SRP S domain with SRP72 RNA-binding domain

Method: X-RAY DIFFRACTION Dmax: 159.8 Å Quality: GOOD

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 × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain B; UniProt 11–118 Not recorded Human gene for small cytoplasmic 7SL RNA (7L30.1) × 1 Signal recognition particle subunit SRP68 × 1 (Q9UHB9) Signal recognition particle subunit SRP72 × 1 (O76094) MG MAGNESIUM ION × 30 K POTASSIUM ION × 5 GOL GLYCEROL × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;17 % (w/v) PEG3350 0.1 M KF 0.1 M Tris pH 8.5 Resolution 3.40 Å R-free 0.280
2 Protein–RNA Heteromer Protein × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain F; UniProt 11–118 Not recorded Human gene for small cytoplasmic 7SL RNA (7L30.1) × 1 Signal recognition particle subunit SRP68 × 1 (Q9UHB9) Signal recognition particle subunit SRP72 × 1 (O76094) MG MAGNESIUM ION × 15 K POTASSIUM ION × 5 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;17 % (w/v) PEG3350 0.1 M KF 0.1 M Tris pH 8.5 Resolution 3.40 Å R-free 0.280

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 8 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 11–118; UniProt 11–118 Author chain F; PDBConstruct 11–118; UniProt 11–118

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 × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain C; UniProt 60–254 Not recorded Human gene for small cytoplasmic 7SL RNA (7L30.1) × 1 Signal recognition particle 19 kDa protein × 1 (P09132) Signal recognition particle subunit SRP72 × 1 (O76094) MG MAGNESIUM ION × 30 K POTASSIUM ION × 5 GOL GLYCEROL × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;17 % (w/v) PEG3350 0.1 M KF 0.1 M Tris pH 8.5 Resolution 3.40 Å R-free 0.280
2 Protein–RNA Heteromer Protein × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain G; UniProt 60–254 Not recorded Human gene for small cytoplasmic 7SL RNA (7L30.1) × 1 Signal recognition particle 19 kDa protein × 1 (P09132) Signal recognition particle subunit SRP72 × 1 (O76094) MG MAGNESIUM ION × 15 K POTASSIUM ION × 5 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;17 % (w/v) PEG3350 0.1 M KF 0.1 M Tris pH 8.5 Resolution 3.40 Å R-free 0.280

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 8 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 9–203; UniProt 60–254 Author chain G; PDBConstruct 9–203; UniProt 60–254

Signal recognition particle subunit SRP72

Homo sapiens

UniProt O76094

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 × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain D; UniProt 512–668 Not recorded Human gene for small cytoplasmic 7SL RNA (7L30.1) × 1 Signal recognition particle 19 kDa protein × 1 (P09132) Signal recognition particle subunit SRP68 × 1 (Q9UHB9) MG MAGNESIUM ION × 30 K POTASSIUM ION × 5 GOL GLYCEROL × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;17 % (w/v) PEG3350 0.1 M KF 0.1 M Tris pH 8.5 Resolution 3.40 Å R-free 0.280
2 Protein–RNA Heteromer Protein × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain H; UniProt 512–668 Not recorded Human gene for small cytoplasmic 7SL RNA (7L30.1) × 1 Signal recognition particle 19 kDa protein × 1 (P09132) Signal recognition particle subunit SRP68 × 1 (Q9UHB9) MG MAGNESIUM ION × 15 K POTASSIUM ION × 5 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;17 % (w/v) PEG3350 0.1 M KF 0.1 M Tris pH 8.5 Resolution 3.40 Å R-free 0.280

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.

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

View Construct and Data Evidence
UniProt name SRP72_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 2–158; UniProt 512–668 Author chain H; PDBConstruct 2–158; UniProt 512–668

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 5m73

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5m73
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5m73
Deposition date deposition_date2016-10-26
Structure title titleStructure of the human SRP S domain with SRP72 RNA-binding domain
Keywords keywordsprotein targeting, signal recognition particle, protein-RNA complex, RNA kink-turn, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier46.60
Radius of gyration Rg (electron density) rg_electron47.66
Forward intensity I(0) i0927867000.00
Molecular weight molecular_weight179120.0 kDa
Excluded volume excluded_volume193620 ų
Envelope volume envelope_volume336580 ų
Hydration-shell volume shell_volume61705 ų
Envelope diameter envelope_diameter167.2
Shell Rg shell_rg48.97
Envelope Rg envelope_rg46.45
Shape Rg shape_rg47.67
Total Rg total_rg47.68
Total atoms total_atoms12128
Residues n_residues982
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 dmax159.8
Rg (real space) rg_real46.74
Rg uncertainty (real space) rg_real_error2.17
I(0) (real space) i0_real9.2790e+08
I(0) uncertainty (real space) i0_real_error1.8520e+07
Rg (reciprocal space) rg_reciprocal46.60
I(0) (reciprocal space) i0_reciprocal927700000.0000
Solution quality estimate total_estimate0.8525
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.4
Skewness Skewness skewness0.421
Kurtosis Kurtosis kurtosis-0.134
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16630000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.765; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.787

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5m73B00
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_id5m73C00
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
Domain ID domain_id5m73F00
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_id5m73G00
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)