1jzy

Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria

Method: X-RAY DIFFRACTION Dmax: 211.7 Å Quality: GOOD

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

Ribosomal Protein L4

OrganismNot specified

UniProt Q9RXK1

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 K; UniProt 1–205 Not recorded 23S rRNA × 1 Ribosomal Protein L22 × 1 (Q9RXJ7) Ribosomal Protein L32 × 1 (P49228) ERY ERYTHROMYCIN A × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;291 K;ethanol, dimethylhexanediol, MgCl2, KCl, Hepes, NH4Cl, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.50 Å R-free 0.301

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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL4_DEIRA
Isoform
PDB entities 2
Chains and sequence ranges Author chain K; PDBConstruct 1–205; UniProt 1–205

Ribosomal Protein L22

OrganismNot specified

UniProt Q9RXJ7

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 L; UniProt 1–134 Not recorded 23S rRNA × 1 Ribosomal Protein L4 × 1 (Q9RXK1) Ribosomal Protein L32 × 1 (P49228) ERY ERYTHROMYCIN A × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;291 K;ethanol, dimethylhexanediol, MgCl2, KCl, Hepes, NH4Cl, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.50 Å R-free 0.301

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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL22_DEIRA
Isoform
PDB entities 3
Chains and sequence ranges Author chain L; PDBConstruct 1–134; UniProt 1–134

Ribosomal Protein L32

OrganismNot specified

UniProt P49228

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 M; UniProt 1–60 Not recorded 23S rRNA × 1 Ribosomal Protein L4 × 1 (Q9RXK1) Ribosomal Protein L22 × 1 (Q9RXJ7) ERY ERYTHROMYCIN A × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;291 K;ethanol, dimethylhexanediol, MgCl2, KCl, Hepes, NH4Cl, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.50 Å R-free 0.301

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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL32_DEIRA
Isoform
PDB entities 4
Chains and sequence ranges Author chain M; PDBConstruct 1–60; UniProt 1–60

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 1jzy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1jzy
Deposition date deposition_date2001-09-17
Structure title titleStructural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria
Keywords keywordsRibosome, 50S, 23S, 5S, Antibiotics, Erythromycin, Peptidyl transferase center; RIBOSOME
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier64.95
Radius of gyration Rg (electron density) rg_electron64.49
Forward intensity I(0) i037340500000.00
Molecular weight molecular_weight945500.0 kDa
Excluded volume excluded_volume892930 ų
Envelope volume envelope_volume1671100 ų
Hydration-shell volume shell_volume201680 ų
Envelope diameter envelope_diameter249.0
Shell Rg shell_rg74.68
Envelope Rg envelope_rg64.19
Shape Rg shape_rg64.49
Total Rg total_rg64.56
Total atoms total_atoms59585
Residues n_residues2774
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 dmax211.7
Rg (real space) rg_real64.58
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real3.7330e+10
I(0) uncertainty (real space) i0_real_error7.4890e+08
Rg (reciprocal space) rg_reciprocal65.23
I(0) (reciprocal space) i0_reciprocal37380000000.0000
Solution quality estimate total_estimate0.8557
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary79.4
Skewness Skewness skewness0.253
Kurtosis Kurtosis kurtosis-0.280
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0037
Highest regularization parameter α highest_alpha3453000000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.829; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.689

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1jzyk_
Class classi — Low resolution protein structures
Fold Fold foldi.1 — Ribosome and ribosomal fragments
Superfamily Superfamily superfamilyi.1.1 — Ribosome and ribosomal fragments
Family Family familyi.1.1.2 — Large subunit
Domain ID domain_idd1jzyl_
Class classi — Low resolution protein structures
Fold Fold foldi.1 — Ribosome and ribosomal fragments
Superfamily Superfamily superfamilyi.1.1 — Ribosome and ribosomal fragments
Family Family familyi.1.1.2 — Large subunit
Domain ID domain_idd1jzym_
Class classi — Low resolution protein structures
Fold Fold foldi.1 — Ribosome and ribosomal fragments
Superfamily Superfamily superfamilyi.1.1 — Ribosome and ribosomal fragments
Family Family familyi.1.1.2 — Large subunit

8. Citations (1)

9. Files and Curves (10)