6pc7

E. coli 50S ribosome bound to compound 46

Method: ELECTRON MICROSCOPY Dmax: 229.5 Å Quality: GOOD

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

50S ribosomal protein L2

OrganismNot specified

UniProt P60422

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 × 5 RNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain K; UniProt 2–272 Not recorded 23S ribosomal RNA × 1 5S ribosomal RNA × 1 50S ribosomal protein L15 × 1 (A0A037Y8L6) 50S ribosomal protein L4 × 1 (D7Z9F6) 50S ribosomal protein L3 × 1 (P60438) 50S ribosomal protein L13 × 1 (D7ZET0) O7V (2R)-2-[(3S,4R,5E,10E,12E,14S,16R,26aR)-16-fluoro-14-hydroxy-4,12-dimethyl-1,7,22-trioxo-4,7,8,9,14,15,16,17,24,25,26,26a-dodecahydro-1H,3H,22H-21,18-(azeno)pyrrolo[2,1-c][1,8,4,19]dioxadiazacyclotetracosin-3-yl]propyl isoquinolin-3-ylcarbamate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.50 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.

624 other PDB entries and 669 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL2_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain K; PDBConstruct 1–271; UniProt 2–272

50S ribosomal protein L15

OrganismNot specified

UniProt A0A037Y8L6

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 × 5 RNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain L; UniProt 1–144 Not recorded 23S ribosomal RNA × 1 5S ribosomal RNA × 1 50S ribosomal protein L2 × 1 (P60422) 50S ribosomal protein L4 × 1 (D7Z9F6) 50S ribosomal protein L3 × 1 (P60438) 50S ribosomal protein L13 × 1 (D7ZET0) O7V (2R)-2-[(3S,4R,5E,10E,12E,14S,16R,26aR)-16-fluoro-14-hydroxy-4,12-dimethyl-1,7,22-trioxo-4,7,8,9,14,15,16,17,24,25,26,26a-dodecahydro-1H,3H,22H-21,18-(azeno)pyrrolo[2,1-c][1,8,4,19]dioxadiazacyclotetracosin-3-yl]propyl isoquinolin-3-ylcarbamate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.50 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.

146 other PDB entries and 146 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A037Y8L6_ECOLX
Isoform
PDB entities 4
Chains and sequence ranges Author chain L; PDBConstruct 1–144; UniProt 1–144

50S ribosomal protein L4

OrganismNot specified

UniProt D7Z9F6

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 × 5 RNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain M; UniProt 1–201 Not recorded 23S ribosomal RNA × 1 5S ribosomal RNA × 1 50S ribosomal protein L2 × 1 (P60422) 50S ribosomal protein L15 × 1 (A0A037Y8L6) 50S ribosomal protein L3 × 1 (P60438) 50S ribosomal protein L13 × 1 (D7ZET0) O7V (2R)-2-[(3S,4R,5E,10E,12E,14S,16R,26aR)-16-fluoro-14-hydroxy-4,12-dimethyl-1,7,22-trioxo-4,7,8,9,14,15,16,17,24,25,26,26a-dodecahydro-1H,3H,22H-21,18-(azeno)pyrrolo[2,1-c][1,8,4,19]dioxadiazacyclotetracosin-3-yl]propyl isoquinolin-3-ylcarbamate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.50 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.

66 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D7Z9F6_ECOLX
Isoform
PDB entities 5
Chains and sequence ranges Author chain M; PDBConstruct 1–201; UniProt 1–201

50S ribosomal protein L3

OrganismNot specified

UniProt P60438

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 × 5 RNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain N; UniProt 1–209 Not recorded 23S ribosomal RNA × 1 5S ribosomal RNA × 1 50S ribosomal protein L2 × 1 (P60422) 50S ribosomal protein L15 × 1 (A0A037Y8L6) 50S ribosomal protein L4 × 1 (D7Z9F6) 50S ribosomal protein L13 × 1 (D7ZET0) O7V (2R)-2-[(3S,4R,5E,10E,12E,14S,16R,26aR)-16-fluoro-14-hydroxy-4,12-dimethyl-1,7,22-trioxo-4,7,8,9,14,15,16,17,24,25,26,26a-dodecahydro-1H,3H,22H-21,18-(azeno)pyrrolo[2,1-c][1,8,4,19]dioxadiazacyclotetracosin-3-yl]propyl isoquinolin-3-ylcarbamate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.50 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.

629 other PDB entries and 674 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL3_ECOLI
Isoform
PDB entities 6
Chains and sequence ranges Author chain N; PDBConstruct 1–209; UniProt 1–209

50S ribosomal protein L13

OrganismNot specified

UniProt D7ZET0

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 × 5 RNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain O; UniProt 1–142 Not recorded 23S ribosomal RNA × 1 5S ribosomal RNA × 1 50S ribosomal protein L2 × 1 (P60422) 50S ribosomal protein L15 × 1 (A0A037Y8L6) 50S ribosomal protein L4 × 1 (D7Z9F6) 50S ribosomal protein L3 × 1 (P60438) O7V (2R)-2-[(3S,4R,5E,10E,12E,14S,16R,26aR)-16-fluoro-14-hydroxy-4,12-dimethyl-1,7,22-trioxo-4,7,8,9,14,15,16,17,24,25,26,26a-dodecahydro-1H,3H,22H-21,18-(azeno)pyrrolo[2,1-c][1,8,4,19]dioxadiazacyclotetracosin-3-yl]propyl isoquinolin-3-ylcarbamate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.50 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.

65 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D7ZET0_ECOLX
Isoform
PDB entities 7
Chains and sequence ranges Author chain O; PDBConstruct 1–142; UniProt 1–142

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 6pc7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6pc7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6pc7
Deposition date deposition_date2019-06-16
Structure title titleE. coli 50S ribosome bound to compound 46
Keywords keywordsE. coli ribosome, streptogramin A analog, antibiotics, RIBOSOME; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier68.48
Radius of gyration Rg (electron density) rg_electron68.27
Forward intensity I(0) i046967800000.00
Molecular weight molecular_weight1086300.0 kDa
Excluded volume excluded_volume1045000 ų
Envelope volume envelope_volume1938900 ų
Hydration-shell volume shell_volume220910 ų
Envelope diameter envelope_diameter236.3
Shell Rg shell_rg78.31
Envelope Rg envelope_rg67.87
Shape Rg shape_rg68.23
Total Rg total_rg68.40
Total atoms total_atoms72146
Residues n_residues3958
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 dmax229.5
Rg (real space) rg_real68.31
Rg uncertainty (real space) rg_real_error2.10
I(0) (real space) i0_real4.6970e+10
I(0) uncertainty (real space) i0_real_error1.0950e+09
Rg (reciprocal space) rg_reciprocal69.00
I(0) (reciprocal space) i0_reciprocal47030000000.0000
Solution quality estimate total_estimate0.8539
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary89.8
Skewness Skewness skewness0.255
Kurtosis Kurtosis kurtosis-0.328
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4658000000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.719

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6pc7L01
Class class3 — Alpha Beta
Architecture architecture100 — Ribosomal Protein L15; Chain: K; domain 2
Topology topology10 — Ribosomal Protein L15; Chain: K; domain 2
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)