2aar

Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome.

Method: X-RAY DIFFRACTION Dmax: 215.6 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 × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain R; UniProt 1–95 Not recorded 23S ribosomal RNA × 1 50S ribosomal protein L29 × 1 (Q9RXJ4) Trigger Factor × 1 (Q9RT21) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;293 K;pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 20K Resolution 3.50 Å R-free 0.320

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 1–95

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 × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain W; UniProt 1–67 Not recorded 23S ribosomal RNA × 1 50S ribosomal protein L23 × 1 (Q9RXK0) Trigger Factor × 1 (Q9RT21) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;293 K;pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 20K Resolution 3.50 Å R-free 0.320

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 3
Chains and sequence ranges Author chain W; PDBConstruct 1–67; UniProt 1–67

Trigger Factor

OrganismNot specified

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 × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain 7; UniProt 1–113 Fragment:N-terminal Domain 23S ribosomal RNA × 1 50S ribosomal protein L23 × 1 (Q9RXK0) 50S ribosomal protein L29 × 1 (Q9RXJ4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;293 K;pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 20K Resolution 3.50 Å R-free 0.320

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 4
Chains and sequence ranges Author chain 7; PDBConstruct 1–113; UniProt 1–113

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 2aar

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2aar
Deposition date deposition_date2005-07-14
Structure title titleStructure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome.
Keywords keywordsTrigger Factor, 50S, ribosome, Cheperone, Tunnel; RIBOSOME
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier65.47
Radius of gyration Rg (electron density) rg_electron65.32
Forward intensity I(0) i036541900000.00
Molecular weight molecular_weight929790.0 kDa
Excluded volume excluded_volume874190 ų
Envelope volume envelope_volume1689600 ų
Hydration-shell volume shell_volume203020 ų
Envelope diameter envelope_diameter248.1
Shell Rg shell_rg74.79
Envelope Rg envelope_rg64.55
Shape Rg shape_rg64.76
Total Rg total_rg66.21
Total atoms total_atoms59359
Residues n_residues2766
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 dmax215.6
Rg (real space) rg_real65.11
Rg uncertainty (real space) rg_real_error1.42
I(0) (real space) i0_real3.6540e+10
I(0) uncertainty (real space) i0_real_error7.2660e+08
Rg (reciprocal space) rg_reciprocal65.75
I(0) (reciprocal space) i0_reciprocal36580000000.0000
Solution quality estimate total_estimate0.7978
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary80.8
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.255
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3385000000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.808; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2aarr1
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_idd2aarw1
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)

8. Citations (1)

9. Files and Curves (10)