1mvr

Decoding Center & Peptidyl transferase center from the X-ray structure of the Thermus thermophilus 70S ribosome, aligned to the low resolution Cryo-EM map of E.coli 70S Ribosome

Method: ELECTRON MICROSCOPY Dmax: 160.9 Å Quality: REASONABLE

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

30S RIBOSOMAL PROTEIN S12

OrganismNot specified

UniProt Q5SHN3

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 × 2 RNA 6 PDB declaration: octameric(8) Consistent with all polymer counts Chain O; UniProt 1–131 Not recorded mRNA, triplet codon (A-site) × 1 Helix 34 of 16S rRNA × 1 Helix 44 of 16S rRNA × 1 Helix 69 of 23S rRNA × 1 Helix 89 of 23S rRNA × 1 Helix 93 of 23S rRNA × 1 50S ribosomal protein L11 × 1 (P29395) ELECTRON MICROSCOPY cryo-EM buffer:polymix buffer;pH 7.5;polymix buffer cryo-EM vitrification conditions:Cryogen ETHANE;Rapid-freezing in liquid ethane Resolution 12.80 Å

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.

323 other PDB entries and 543 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS12_THET8
Isoform
PDB entities 7
Chains and sequence ranges Author chain O; PDBConstruct 5–135; UniProt 1–131

50S ribosomal protein L11

OrganismNot specified

UniProt P29395

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 × 2 RNA 6 PDB declaration: octameric(8) Consistent with all polymer counts Chain L; UniProt 1–140 Not recorded mRNA, triplet codon (A-site) × 1 Helix 34 of 16S rRNA × 1 Helix 44 of 16S rRNA × 1 Helix 69 of 23S rRNA × 1 Helix 89 of 23S rRNA × 1 Helix 93 of 23S rRNA × 1 30S RIBOSOMAL PROTEIN S12 × 1 (Q5SHN3) ELECTRON MICROSCOPY cryo-EM buffer:polymix buffer;pH 7.5;polymix buffer cryo-EM vitrification conditions:Cryogen ETHANE;Rapid-freezing in liquid ethane Resolution 12.80 Å

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.

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

View Construct and Data Evidence
UniProt name RL11_THEMA
Isoform
PDB entities 8
Chains and sequence ranges Author chain L; PDBConstruct 1–140; UniProt 1–140

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 1mvr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1mvr
Deposition date deposition_date2002-09-26
Structure title titleDecoding Center & Peptidyl transferase center from the X-ray structure of the Thermus thermophilus 70S ribosome, aligned to the low resolution Cryo-EM map of E.coli 70S Ribosome
Keywords keywordsRF2, Release Complex, Conformational Changes, RIBOSOME; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.70
Radius of gyration Rg (electron density) rg_electron49.94
Forward intensity I(0) i045685500.00
Molecular weight molecular_weight35756.0 kDa
Excluded volume excluded_volume36309 ų
Envelope volume envelope_volume137570 ų
Hydration-shell volume shell_volume24494 ų
Envelope diameter envelope_diameter164.7
Shell Rg shell_rg50.10
Envelope Rg envelope_rg48.14
Shape Rg shape_rg52.61
Total Rg total_rg49.76
Total atoms total_atoms249
Residues n_residues249
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 dmax160.9
Rg (real space) rg_real52.61
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real4.5680e+07
I(0) uncertainty (real space) i0_real_error8.8840e+05
Rg (reciprocal space) rg_reciprocal52.76
I(0) (reciprocal space) i0_reciprocal45690000.0000
Solution quality estimate total_estimate0.6077
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary75.1
Skewness Skewness skewness-0.013
Kurtosis Kurtosis kurtosis-0.516
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha4369000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.762; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.996; Smooth: 0.428

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1mvrl_
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.1.1.1 — Ribosome complexes
Domain ID domain_idd1mvro_
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.1.1.1 — Ribosome complexes

8. Citations (3)

9. Files and Curves (10)