1bxe

RIBOSOMAL PROTEIN L22 FROM THERMUS THERMOPHILUS

Method: X-RAY DIFFRACTION Dmax: 71.1 Å Quality: REASONABLE

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

PROTEIN (RIBOSOMAL PROTEIN L22)

Thermus thermophilus

UniProt P48286

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 1–113 Mutation:MET1MSE, MET64MSE Non-standard monomer:Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;pH 7 Resolution 1.90 Å R-free 0.219

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.

16 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL22_THETH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; 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 1bxe

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bxe
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bxe
Deposition date deposition_date1998-10-02
Structure title titleRIBOSOMAL PROTEIN L22 FROM THERMUS THERMOPHILUS
Keywords keywordsRIBOSOMAL PROTEIN, PROTEIN SYNTHESIS, RNA BINDING, ANTIBIOTICS RESISTANCE, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.16
Radius of gyration Rg (electron density) rg_electron17.46
Forward intensity I(0) i03282490.00
Molecular weight molecular_weight12654.0 kDa
Excluded volume excluded_volume15858 ų
Envelope volume envelope_volume19600 ų
Hydration-shell volume shell_volume10977 ų
Envelope diameter envelope_diameter70.3
Shell Rg shell_rg21.37
Envelope Rg envelope_rg18.77
Shape Rg shape_rg17.42
Total Rg total_rg18.34
Total atoms total_atoms879
Residues n_residues108
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 dmax71.1
Rg (real space) rg_real18.63
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real3.2820e+06
I(0) uncertainty (real space) i0_real_error4.3740e+04
Rg (reciprocal space) rg_reciprocal18.57
I(0) (reciprocal space) i0_reciprocal3282000.0000
Solution quality estimate total_estimate0.7226
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.3
Skewness Skewness skewness0.897
Kurtosis Kurtosis kurtosis0.593
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha739300.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.378; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.309; Smooth: 0.948

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bxea_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.55 — Ribosomal protein L22
Superfamily Superfamily superfamilyd.55.1 — Ribosomal protein L22
Family Family familyd.55.1.1 — Ribosomal protein L22

CATH v4.4 (1 domains)

Domain ID domain_id1bxeA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology470 — Ribosomal Protein L22; Chain A
Homologous superfamily homologous superfamily10 — Ribosomal protein L22/L17

8. Citations (1)

9. Files and Curves (10)