5npm

CRYSTAL STRUCTURE OF MUTANT RIBOSOMAL PROTEIN TTHL1 LACKING 8 N-TERMINAL RESIDUES IN COMPLEX WITH 80NT 23S RNA FROM THERMUS THERMOPHILUS

Method: X-RAY DIFFRACTION Dmax: 79.7 Å Quality: REASONABLE

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

50S ribosomal protein L1

Thermus thermophilus

UniProt P27150

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 Monomer Protein × 1 RNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain A; UniProt 10–229 Not recorded 23S ribosomal RNA × 1 MLI MALONATE ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;295 K;2.4 M sodium malonate Resolution 2.70 Å R-free 0.249

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.

39 other PDB entries and 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL1_THETH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–220; UniProt 10–229

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 5npm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5npm
Deposition date deposition_date2017-04-17
Structure title titleCRYSTAL STRUCTURE OF MUTANT RIBOSOMAL PROTEIN TTHL1 LACKING 8 N-TERMINAL RESIDUES IN COMPLEX WITH 80NT 23S RNA FROM THERMUS THERMOPHILUS
Keywords keywordsribosome, 50S, 23S rRNA, L1 stalk, RNA; RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.52
Radius of gyration Rg (electron density) rg_electron23.39
Forward intensity I(0) i075654000.00
Molecular weight molecular_weight48936.0 kDa
Excluded volume excluded_volume53027 ų
Envelope volume envelope_volume71284 ų
Hydration-shell volume shell_volume25937 ų
Envelope diameter envelope_diameter81.7
Shell Rg shell_rg30.03
Envelope Rg envelope_rg23.17
Shape Rg shape_rg23.36
Total Rg total_rg24.02
Total atoms total_atoms3331
Residues n_residues291
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 dmax79.7
Rg (real space) rg_real23.47
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real7.5650e+07
I(0) uncertainty (real space) i0_real_error9.1080e+05
Rg (reciprocal space) rg_reciprocal23.48
I(0) (reciprocal space) i0_reciprocal75650000.0000
Solution quality estimate total_estimate0.6680
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.4
Skewness Skewness skewness0.318
Kurtosis Kurtosis kurtosis-0.196
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha5029000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.780; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.997; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5npmA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology190 — Ribulose 1,5 Bisphosphate Carboxylase/Oxygenase
Homologous superfamily homologous superfamily20 — Ribosomal protein L1/L10, rRNA-binding domain
Domain ID domain_id5npmA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily790 — Ribosomal protein L1/L10, domain II

8. Citations (1)

9. Files and Curves (10)