487d

SEVEN RIBOSOMAL PROTEINS FITTED TO A CRYO-ELECTRON MICROSCOPIC MAP OF THE LARGE 50S SUBUNIT AT 7.5 ANGSTROMS RESOLUTION

Method: ELECTRON MICROSCOPY Dmax: 308.0 Å Quality: REASONABLE

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

50S ribosomal protein L1

OrganismNot specified

UniProt P27150

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain H; UniProt 6–229 Not recorded 50S ribosomal protein L2 × 1 (P04257) 50S ribosomal protein L6 × 1 (P02391) 50S ribosomal protein L9 × 1 (P02417) 50S ribosomal protein L11 × 1 (P29395) 50S ribosomal protein L14 × 1 (P04450) 50S ribosomal protein L25 × 1 (C3T3H7) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 7.50 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.

39 other PDB entries and 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL1_THETH
Isoform
PDB entities 1
Chains and sequence ranges Author chain H; PDBConstruct 1–224; UniProt 6–229

50S ribosomal protein L2

OrganismNot specified

UniProt P04257

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain I; UniProt 61–195 Non-standard monomer:Yes (specific site not provided by mmCIF) 50S ribosomal protein L1 × 1 (P27150) 50S ribosomal protein L6 × 1 (P02391) 50S ribosomal protein L9 × 1 (P02417) 50S ribosomal protein L11 × 1 (P29395) 50S ribosomal protein L14 × 1 (P04450) 50S ribosomal protein L25 × 1 (C3T3H7) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 7.50 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.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL2_GEOSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–135; UniProt 61–195

50S ribosomal protein L6

OrganismNot specified

UniProt P02391

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain J; UniProt 8–171 Not recorded 50S ribosomal protein L1 × 1 (P27150) 50S ribosomal protein L2 × 1 (P04257) 50S ribosomal protein L9 × 1 (P02417) 50S ribosomal protein L11 × 1 (P29395) 50S ribosomal protein L14 × 1 (P04450) 50S ribosomal protein L25 × 1 (C3T3H7) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 7.50 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL6_GEOSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 1–164; UniProt 8–171

50S ribosomal protein L9

OrganismNot specified

UniProt P02417

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain K; UniProt 1–149 Not recorded 50S ribosomal protein L1 × 1 (P27150) 50S ribosomal protein L2 × 1 (P04257) 50S ribosomal protein L6 × 1 (P02391) 50S ribosomal protein L11 × 1 (P29395) 50S ribosomal protein L14 × 1 (P04450) 50S ribosomal protein L25 × 1 (C3T3H7) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 7.50 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.

6 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL9_GEOSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain K; PDBConstruct 1–149; UniProt 1–149

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain L; UniProt 8–140 Not recorded 50S ribosomal protein L1 × 1 (P27150) 50S ribosomal protein L2 × 1 (P04257) 50S ribosomal protein L6 × 1 (P02391) 50S ribosomal protein L9 × 1 (P02417) 50S ribosomal protein L14 × 1 (P04450) 50S ribosomal protein L25 × 1 (C3T3H7) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 7.50 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.

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 5
Chains and sequence ranges Author chain L; PDBConstruct 1–133; UniProt 8–140

50S ribosomal protein L14

OrganismNot specified

UniProt P04450

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain M; UniProt 1–122 Not recorded 50S ribosomal protein L1 × 1 (P27150) 50S ribosomal protein L2 × 1 (P04257) 50S ribosomal protein L6 × 1 (P02391) 50S ribosomal protein L9 × 1 (P02417) 50S ribosomal protein L11 × 1 (P29395) 50S ribosomal protein L25 × 1 (C3T3H7) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 7.50 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL14_GEOSE
Isoform
PDB entities 6
Chains and sequence ranges Author chain M; PDBConstruct 1–122; UniProt 1–122

50S ribosomal protein L25

OrganismNot specified

UniProt C3T3H7

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain N; UniProt 1–94 Not recorded 50S ribosomal protein L1 × 1 (P27150) 50S ribosomal protein L2 × 1 (P04257) 50S ribosomal protein L6 × 1 (P02391) 50S ribosomal protein L9 × 1 (P02417) 50S ribosomal protein L11 × 1 (P29395) 50S ribosomal protein L14 × 1 (P04450) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 7.50 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3T3H7_ECOLX
Isoform
PDB entities 7
Chains and sequence ranges Author chain N; PDBConstruct 1–94; UniProt 1–94

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 487d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 487d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id487d
Deposition date deposition_date2000-02-23
Structure title titleSEVEN RIBOSOMAL PROTEINS FITTED TO A CRYO-ELECTRON MICROSCOPIC MAP OF THE LARGE 50S SUBUNIT AT 7.5 ANGSTROMS RESOLUTION
Keywords keywords;RIBOSOME, LARGE RIBOSOMAL SUBUNIT, RIBOSOMAL PROTEIN, PROTEIN BIOSYNTHESIS, EM-RECONSTRUCTION, ATOMIC STRUCTURE, 3D ARRANGEMENT, FITTING ;; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier95.46
Radius of gyration Rg (electron density) rg_electron95.86
Forward intensity I(0) i0164285000.00
Molecular weight molecular_weight111430.0 kDa
Excluded volume excluded_volume140930 ų
Envelope volume envelope_volume432190 ų
Hydration-shell volume shell_volume38906 ų
Envelope diameter envelope_diameter246.6
Shell Rg shell_rg101.50
Envelope Rg envelope_rg82.21
Shape Rg shape_rg95.89
Total Rg total_rg95.85
Total atoms total_atoms8778
Residues n_residues1018
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 dmax308.0
Rg (real space) rg_real95.85
Rg uncertainty (real space) rg_real_error4.96
I(0) (real space) i0_real1.6430e+08
I(0) uncertainty (real space) i0_real_error4.5420e+06
Rg (reciprocal space) rg_reciprocal91.40
I(0) (reciprocal space) i0_reciprocal162000000.0000
Solution quality estimate total_estimate0.6040
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary173.2
Skewness Skewness skewness-0.071
Kurtosis Kurtosis kurtosis-1.380
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21170000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.000; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.852; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd487dh_
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_idd487di_
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_idd487dj_
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_idd487dk_
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_idd487dl_
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_idd487dm_
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_idd487dn_
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 (9)

9. Files and Curves (10)