1i4j

CRYSTAL STRUCTURE OF L22 RIBOSOMAL PROTEIN MUTANT

Method: X-RAY DIFFRACTION Dmax: 85.6 Å Quality: GOOD

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

50S 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–113 Chain B; UniProt 1–113 Mutation:DEL(82-84) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;1.9M Sodium chloride, 3% ethanol, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 1.80 Å R-free 0.255

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 1–110; UniProt 1–113 Author chain B; PDBConstruct 1–110; 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 1i4j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1i4j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1i4j
Deposition date deposition_date2001-02-22
Structure title titleCRYSTAL STRUCTURE OF L22 RIBOSOMAL PROTEIN MUTANT
Keywords keywordsRibosomal Protein, Mutant, Erythromycin Resistance, RNA binding, 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_guinier20.89
Radius of gyration Rg (electron density) rg_electron19.96
Forward intensity I(0) i010959200.00
Molecular weight molecular_weight24667.0 kDa
Excluded volume excluded_volume31138 ų
Envelope volume envelope_volume39349 ų
Hydration-shell volume shell_volume17413 ų
Envelope diameter envelope_diameter86.0
Shell Rg shell_rg25.39
Envelope Rg envelope_rg20.93
Shape Rg shape_rg19.94
Total Rg total_rg20.88
Total atoms total_atoms1738
Residues n_residues220
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 dmax85.6
Rg (real space) rg_real21.04
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real1.0960e+07
I(0) uncertainty (real space) i0_real_error1.5920e+05
Rg (reciprocal space) rg_reciprocal21.01
I(0) (reciprocal space) i0_reciprocal10960000.0000
Solution quality estimate total_estimate0.7534
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.659
Kurtosis Kurtosis kurtosis0.685
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2855000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.405; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.585; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1i4ja_
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
Domain ID domain_idd1i4jb_
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 (2 domains)

Domain ID domain_id1i4jA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology470 — Ribosomal Protein L22; Chain A
Homologous superfamily homologous superfamily10 — Ribosomal protein L22/L17
Domain ID domain_id1i4jB00
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)