5d8h

CRYSTAL STRUCTURE OF THE BASE OF THE RIBOSOMAL P STALK FROM METHANOCOCCUS JANNASCHII WITH ANTIBIOTIC THIOSTREPTON

Method: X-RAY DIFFRACTION Dmax: 83.5 Å Quality: EXCELLENT

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

50S ribosomal protein L10

Methanocaldococcus jannaschii

UniProt P54049

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 9–221 Fragment:UNP residues 9-221 Mutation:Met changed to SeMet Non-standard monomer:Yes (specific site not provided by mmCIF) 23S ribosomal RNA × 1 50S ribosomal protein L11 × 1 (P54030) THIOSTREPTON × 1 (P0C8P8) MG MAGNESIUM ION × 11 NA SODIUM ION × 4 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;0.1 mM Tris-HCl, pH 7.5, 10% PEG 8000, 20% glycerol, 1 mM TCEP (tris(2-carboxyethyl)phosphine), 0.125 mM CTAB Resolution 2.80 Å R-free 0.245

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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL10_METJA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–213; UniProt 9–221

50S ribosomal protein L11

Methanocaldococcus jannaschii

UniProt P54030

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 1–161 Non-standard monomer:Yes (specific site not provided by mmCIF) 23S ribosomal RNA × 1 50S ribosomal protein L10 × 1 (P54049) THIOSTREPTON × 1 (P0C8P8) MG MAGNESIUM ION × 11 NA SODIUM ION × 4 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;0.1 mM Tris-HCl, pH 7.5, 10% PEG 8000, 20% glycerol, 1 mM TCEP (tris(2-carboxyethyl)phosphine), 0.125 mM CTAB Resolution 2.80 Å R-free 0.245

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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL11_METJA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–161; UniProt 1–161

THIOSTREPTON

OrganismNot specified

UniProt P0C8P8

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 0–18 Non-standard monomer:Yes (specific site not provided by mmCIF) 23S ribosomal RNA × 1 50S ribosomal protein L10 × 1 (P54049) 50S ribosomal protein L11 × 1 (P54030) MG MAGNESIUM ION × 11 NA SODIUM ION × 4 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;0.1 mM Tris-HCl, pH 7.5, 10% PEG 8000, 20% glycerol, 1 mM TCEP (tris(2-carboxyethyl)phosphine), 0.125 mM CTAB Resolution 2.80 Å R-free 0.245

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.

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

View Construct and Data Evidence
UniProt name THCL_STRAJ
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–19; UniProt 0–18

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 5d8h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5d8h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5d8h
Deposition date deposition_date2015-08-17
Structure title titleCRYSTAL STRUCTURE OF THE BASE OF THE RIBOSOMAL P STALK FROM METHANOCOCCUS JANNASCHII WITH ANTIBIOTIC THIOSTREPTON
Keywords keywordsribosome, P-stalk, archaea, ANTIBIOTIC, THIOSTREPTON, ribosomal protein; RIBOSOMAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.13
Radius of gyration Rg (electron density) rg_electron26.24
Forward intensity I(0) i0111252000.00
Molecular weight molecular_weight66739.0 kDa
Excluded volume excluded_volume76400 ų
Envelope volume envelope_volume102100 ų
Hydration-shell volume shell_volume32159 ų
Envelope diameter envelope_diameter86.6
Shell Rg shell_rg33.73
Envelope Rg envelope_rg26.08
Shape Rg shape_rg26.28
Total Rg total_rg26.79
Total atoms total_atoms4527
Residues n_residues434
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 dmax83.5
Rg (real space) rg_real26.04
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real1.1130e+08
I(0) uncertainty (real space) i0_real_error1.4620e+06
Rg (reciprocal space) rg_reciprocal26.07
I(0) (reciprocal space) i0_reciprocal111300000.0000
Solution quality estimate total_estimate0.9028
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.9
Skewness Skewness skewness0.205
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10340000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id5d8hB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily1730 — Ribosomal protein L10, N-terminal RNA-binding domain
Domain ID domain_id5d8hB02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology105 — Molybdopterin biosynthesis moea protein, domain 2
Homologous superfamily homologous superfamily20 — Ribosomal protein L10, N-terminal fragment, domain II
Domain ID domain_id5d8hC01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1550 — Ribosomal protein L11, N-terminal domain
Homologous superfamily homologous superfamily10 — Ribosomal protein L11/L12, N-terminal domain

8. Citations (1)

9. Files and Curves (10)