2d3o

Structure of Ribosome Binding Domain of the Trigger Factor on the 50S ribosomal subunit from D. radiodurans

Method: X-RAY DIFFRACTION Dmax: 256.3 Å Quality: GOOD

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

50S RIBOSOMAL PROTEIN L23

OrganismNot specified

UniProt Q9RXK0

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 × 4 RNA 1 PDB declaration: pentameric(5) Consistent with all polymer counts Chain R; UniProt 0–94 Not recorded 23S RIBOSOMAL RNA × 1 50S RIBOSOMAL PROTEIN L24 × 1 (Q9RXJ1) 50S RIBOSOMAL PROTEIN L29 × 1 (Q9RXJ4) Trigger Factor × 1 (Q9RT21) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.8;290 K;ETHANOL, DIMETHYLHEXANEDIOL, MGCL2, KCL, HEPES, NH4CL, pH 7.8, VAPOR DIFFUSION, SITTING DROP, temperature 290K Resolution 3.35 Å R-free 0.322

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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL23_DEIRA
Isoform
PDB entities 2
Chains and sequence ranges Author chain R; PDBConstruct 1–95; UniProt 0–94

50S RIBOSOMAL PROTEIN L24

OrganismNot specified

UniProt Q9RXJ1

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 × 4 RNA 1 PDB declaration: pentameric(5) Consistent with all polymer counts Chain S; UniProt 1–115 Not recorded 23S RIBOSOMAL RNA × 1 50S RIBOSOMAL PROTEIN L23 × 1 (Q9RXK0) 50S RIBOSOMAL PROTEIN L29 × 1 (Q9RXJ4) Trigger Factor × 1 (Q9RT21) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.8;290 K;ETHANOL, DIMETHYLHEXANEDIOL, MGCL2, KCL, HEPES, NH4CL, pH 7.8, VAPOR DIFFUSION, SITTING DROP, temperature 290K Resolution 3.35 Å R-free 0.322

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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL24_DEIRA
Isoform
PDB entities 3
Chains and sequence ranges Author chain S; PDBConstruct 1–115; UniProt 1–115

50S RIBOSOMAL PROTEIN L29

OrganismNot specified

UniProt Q9RXJ4

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 × 4 RNA 1 PDB declaration: pentameric(5) Consistent with all polymer counts Chain W; UniProt 1–67 Not recorded 23S RIBOSOMAL RNA × 1 50S RIBOSOMAL PROTEIN L23 × 1 (Q9RXK0) 50S RIBOSOMAL PROTEIN L24 × 1 (Q9RXJ1) Trigger Factor × 1 (Q9RT21) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.8;290 K;ETHANOL, DIMETHYLHEXANEDIOL, MGCL2, KCL, HEPES, NH4CL, pH 7.8, VAPOR DIFFUSION, SITTING DROP, temperature 290K Resolution 3.35 Å R-free 0.322

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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL29_DEIRA
Isoform
PDB entities 4
Chains and sequence ranges Author chain W; PDBConstruct 1–67; UniProt 1–67

Trigger Factor

Deinococcus radiodurans

UniProt Q9RT21

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 × 4 RNA 1 PDB declaration: pentameric(5) Consistent with all polymer counts Chain 1; UniProt 0–111 Fragment:Ribosome Binding domain 23S RIBOSOMAL RNA × 1 50S RIBOSOMAL PROTEIN L23 × 1 (Q9RXK0) 50S RIBOSOMAL PROTEIN L24 × 1 (Q9RXJ1) 50S RIBOSOMAL PROTEIN L29 × 1 (Q9RXJ4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.8;290 K;ETHANOL, DIMETHYLHEXANEDIOL, MGCL2, KCL, HEPES, NH4CL, pH 7.8, VAPOR DIFFUSION, SITTING DROP, temperature 290K Resolution 3.35 Å R-free 0.322

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIG_DEIRA
Isoform
PDB entities 5
Chains and sequence ranges Author chain 1; PDBConstruct 1–112; UniProt 0–111

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 2d3o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2d3o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2d3o
Deposition date deposition_date2005-09-30
Structure title titleStructure of Ribosome Binding Domain of the Trigger Factor on the 50S ribosomal subunit from D. radiodurans
Keywords keywordsRibosome, Trigger Factor, Nascent Chain, 50S, Protein Folding, SRP; RIBOSOME
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier66.62
Radius of gyration Rg (electron density) rg_electron66.45
Forward intensity I(0) i037948100000.00
Molecular weight molecular_weight951920.0 kDa
Excluded volume excluded_volume898970 ų
Envelope volume envelope_volume1785100 ų
Hydration-shell volume shell_volume210450 ų
Envelope diameter envelope_diameter242.9
Shell Rg shell_rg75.95
Envelope Rg envelope_rg66.09
Shape Rg shape_rg66.43
Total Rg total_rg66.54
Total atoms total_atoms63004
Residues n_residues3171
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 dmax256.3
Rg (real space) rg_real70.13
Rg uncertainty (real space) rg_real_error1.71
I(0) (real space) i0_real3.8180e+10
I(0) uncertainty (real space) i0_real_error7.9890e+08
Rg (reciprocal space) rg_reciprocal66.88
I(0) (reciprocal space) i0_reciprocal37990000000.0000
Solution quality estimate total_estimate0.8561
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary85.4
Skewness Skewness skewness0.672
Kurtosis Kurtosis kurtosis0.693
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.8482
Highest regularization parameter α highest_alpha3790000000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.550; Stabil: 0.867; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.907

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2d3or1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.12 — Ribosomal proteins S24e, L23 and L15e
Superfamily Superfamily superfamilyd.12.1 — Ribosomal proteins S24e, L23 and L15e
Family Family familyd.12.1.1 — L23p
Domain ID domain_idd2d3os1
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.5 — Translation proteins SH3-like domain
Family Family familyb.34.5.1 — Ribosomal proteins L24p and L21e
Domain ID domain_idd2d3ow1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.2 — Ribosomal protein L29 (L29p)
Family Family familya.2.2.1 — Ribosomal protein L29 (L29p)

CATH v4.4 (3 domains)

Domain ID domain_id2d3o100
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily1050 — Trigger factor ribosome-binding domain
Domain ID domain_id2d3oR00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain
Domain ID domain_id2d3oW00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily310

8. Citations (1)

9. Files and Curves (10)