4qgb

Crystal structure of mutant ribosomal protein G219V TthL1

Method: X-RAY DIFFRACTION Dmax: 69.7 Å Quality: EXCELLENT

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 14–229 Mutation:G219V CL CHLORIDE ION × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;293 K;2 M ammonium sulfate, 0.1 M sodium acetate, 0.5 l 0.65% polyacrylic acid 5100 sodium salt, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.251
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 14–229 Mutation:G219V CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;293 K;2 M ammonium sulfate, 0.1 M sodium acetate, 0.5 l 0.65% polyacrylic acid 5100 sodium salt, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.251
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 14–229 Chain B; UniProt 14–229 Mutation:G219V CL CHLORIDE ION × 3 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;293 K;2 M ammonium sulfate, 0.1 M sodium acetate, 0.5 l 0.65% polyacrylic acid 5100 sodium salt, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.251

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 53 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 1–216; UniProt 14–229 Author chain B; PDBConstruct 1–216; UniProt 14–229

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 4qgb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4qgb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4qgb
Deposition date deposition_date2014-05-22
Structure title titleCrystal structure of mutant ribosomal protein G219V TthL1
Keywords keywordsRossmann Fold, RIBOSOMAL PROTEIN, rRNA BINDING, RIBOSOME; RIBOSOMAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.23
Radius of gyration Rg (electron density) rg_electron21.90
Forward intensity I(0) i035858000.00
Molecular weight molecular_weight46745.0 kDa
Excluded volume excluded_volume58892 ų
Envelope volume envelope_volume69872 ų
Hydration-shell volume shell_volume26085 ų
Envelope diameter envelope_diameter71.8
Shell Rg shell_rg29.17
Envelope Rg envelope_rg21.86
Shape Rg shape_rg21.91
Total Rg total_rg22.75
Total atoms total_atoms3291
Residues n_residues432
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 dmax69.7
Rg (real space) rg_real23.08
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real3.5860e+07
I(0) uncertainty (real space) i0_real_error4.1330e+05
Rg (reciprocal space) rg_reciprocal23.11
I(0) (reciprocal space) i0_reciprocal35860000.0000
Solution quality estimate total_estimate0.9122
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.0
Skewness Skewness skewness0.104
Kurtosis Kurtosis kurtosis-0.546
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10500000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.958; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4qgbA01
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_id4qgbA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily790 — Ribosomal protein L1/L10, domain II
Domain ID domain_id4qgbB01
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_id4qgbB02
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)