+
Open data
-
Basic information
| Entry | Database: PDB / ID: 4v6a | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Title | Structure of EF-P bound to the 70S ribosome. | |||||||||
Components |
| |||||||||
Keywords | RIBOSOME / translation / elongation factor / initiation / L1-stalk | |||||||||
| Function / homology | Function and homology informationpeptide biosynthetic process / translation elongation factor activity / large ribosomal subunit / regulation of translation / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / small ribosomal subunit rRNA binding ...peptide biosynthetic process / translation elongation factor activity / large ribosomal subunit / regulation of translation / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / small ribosomal subunit rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / zinc ion binding / metal ion binding / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() Thermus thermophilus HB8 (bacteria)![]() ![]() Thermus thermophilus (bacteria) | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.1 Å | |||||||||
Authors | Stanley, R.E. / Blaha, G. | |||||||||
Citation | Journal: Science / Year: 2009Title: Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome. Authors: Blaha, G. / Stanley, R.E. / Steitz, T.A. | |||||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 4v6a.cif.gz | 7.2 MB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb4v6a.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 4v6a.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4v6a_validation.pdf.gz | 1.8 MB | Display | wwPDB validaton report |
|---|---|---|---|---|
| Full document | 4v6a_full_validation.pdf.gz | 4.1 MB | Display | |
| Data in XML | 4v6a_validation.xml.gz | 937.3 KB | Display | |
| Data in CIF | 4v6a_validation.cif.gz | 1.3 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v6/4v6a ftp://data.pdbj.org/pub/pdb/validation_reports/v6/4v6a | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 2j00 ![]() 2j01 S: Starting model for refinement |
|---|---|
| Similar structure data |
-
Links
-
Assembly
| Deposited unit | ![]()
| ||||||||
|---|---|---|---|---|---|---|---|---|---|
| 1 | ![]()
| ||||||||
| 2 | ![]()
| ||||||||
| Unit cell |
|
-
Components
-RNA chain , 5 types, 10 molecules AACAAWCWAXCXBADABBDB
| #1: RNA chain | Mass: 489961.031 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: GenBank: 55771382#23: RNA chain | Mass: 24802.785 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #24: RNA chain | Mass: 1594.032 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: chemical synthesis #25: RNA chain | Mass: 947895.375 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: GenBank: 55771382#26: RNA chain | Mass: 39494.535 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: GenBank: 55771382 |
|---|
-30S ribosomal protein ... , 20 types, 40 molecules ABCBACCCADCDAECEAFCFAGCGAHCHAICIAJCJAKCKALCLAMCMANCNAOCOAPCP...
| #2: Protein | Mass: 29317.703 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80371#3: Protein | Mass: 26751.076 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80372#4: Protein | Mass: 24373.447 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80373#5: Protein | Mass: 17583.416 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHQ5#6: Protein | Mass: 11988.753 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SLP8#7: Protein | Mass: 18050.973 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P17291#8: Protein | Mass: 15868.570 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHQ2, UniProt: A0A0M9AFS9*PLUS#9: Protein | Mass: 14410.614 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80374#10: Protein | Mass: 11954.968 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHN7#11: Protein | Mass: 13737.868 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80376#12: Protein | Mass: 14637.384 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHN3#13: Protein | Mass: 14338.861 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80377#14: Protein | Mass: 7158.725 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHQ1, UniProt: A0A0N0BLP2*PLUS#15: Protein | Mass: 10578.407 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SJ76#16: Protein | Mass: 10409.983 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SJH3#17: Protein | Mass: 12325.655 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHP7, UniProt: A0A0N0BLS5*PLUS#18: Protein | Mass: 10258.299 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SLQ0#19: Protein | Mass: 10605.464 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHP2#20: Protein | Mass: 11736.143 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80380#21: Protein/peptide | Mass: 3350.030 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SIH3 |
|---|
-Protein , 1 types, 2 molecules AVCV
| #22: Protein | Mass: 20247.010 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Thermus thermophilus HB8 (bacteria) / Strain: AT-62 / Gene: efp, TTHA1125 / Plasmid: pET14b / Production host: ![]() |
|---|
+50S ribosomal protein ... , 30 types, 60 molecules BCDCBDDDBEDEBFDFBGDGBHDHBIDIBNDNBODOBPDPBQDQBRDRBSDSBTDTBUDU...
-Non-polymers , 2 types, 1056 molecules 


| #57: Chemical | ChemComp-MG / #58: Chemical | ChemComp-ZN / |
|---|
-Details
| Has protein modification | Y |
|---|
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
|---|
-
Sample preparation
| Crystal | Density Matthews: 3.26 Å3/Da / Density % sol: 62.28 % |
|---|---|
| Crystal grow | Temperature: 292 K / Method: vapor diffusion / pH: 7.6 Details: 0.1-0.2 M Arginine-HCL, 0.1 M Tris pH 7.6, 2.5 % Peg 20K, 7-12% MPD, 0.5 mM BME, vapor diffusion, temperature 292K |
-Data collection
| Diffraction | Mean temperature: 100 K |
|---|---|
| Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.97949 Å |
| Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Dec 4, 2008 |
| Radiation | Monochromator: Kohzu HLD8-24 monochromator / Protocol: SINGLE WAVELENGTH / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.97949 Å / Relative weight: 1 |
| Reflection | Highest resolution: 3.1 Å / Num. obs: 989777 / % possible obs: 92.2 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 71.4 Å2 / Rmerge(I) obs: 0.258 |
| Reflection shell | Resolution: 3.1→3.18 Å / Rmerge(I) obs: 0.012 / Mean I/σ(I) obs: 0.8 / Num. measured obs: 93519 / Num. unique all: 1048227 / Num. unique obs: 38341 / % possible all: 49.6 |
-Phasing
| Phasing | Method: molecular replacement |
|---|
-
Processing
| Software |
| ||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB Entries: 2j00, 2j01 Highest resolution: 3.1 Å / Occupancy max: 1 / Occupancy min: 0.2 / FOM work R set: 0.752 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 1 / σ(I): 1 / Stereochemistry target values: Engh & Huber / Details: weighted least square procedure
| ||||||||||||||||||||||||||||
| Displacement parameters | Biso max: 205.18 Å2 / Biso mean: 71.935 Å2 / Biso min: 6.18 Å2 | ||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Highest resolution: 3.1 Å
| ||||||||||||||||||||||||||||
| Refine LS restraints |
|
Movie
Controller
About Yorodumi





Thermus thermophilus HB8 (bacteria)
X-RAY DIFFRACTION
Citation










PDBj

































