1k01

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

Method: X-RAY DIFFRACTION Dmax: 214.5 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) MG MAGNESIUM ION × 3 CLM CHLORAMPHENICOL × 1 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 0.321

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) MG MAGNESIUM ION × 3 CLM CHLORAMPHENICOL × 1 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 0.321

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) MG MAGNESIUM ION × 3 CLM CHLORAMPHENICOL × 1 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 0.321

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 1k01

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1k01
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1k01
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, Chloramphenicol, 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_guinier64.94
Radius of gyration Rg (electron density) rg_electron64.50
Forward intensity I(0) i037347200000.00
Molecular weight molecular_weight945110.0 kDa
Excluded volume excluded_volume892220 ų
Envelope volume envelope_volume1671500 ų
Hydration-shell volume shell_volume201720 ų
Envelope diameter envelope_diameter249.0
Shell Rg shell_rg74.68
Envelope Rg envelope_rg64.20
Shape Rg shape_rg64.51
Total Rg total_rg64.57
Total atoms total_atoms59555
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 dmax214.5
Rg (real space) rg_real64.59
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real3.7350e+10
I(0) uncertainty (real space) i0_real_error7.5620e+08
Rg (reciprocal space) rg_reciprocal65.22
I(0) (reciprocal space) i0_reciprocal37390000000.0000
Solution quality estimate total_estimate0.8561
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary80.5
Skewness Skewness skewness0.256
Kurtosis Kurtosis kurtosis-0.273
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3478000000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.806; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.946; Smooth: 0.762

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_idd1k01k_
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_idd1k01l_
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_idd1k01m_
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)