2ov7

The first domain of the ribosomal protein L1 from Thermus thermophilus

Method: X-RAY DIFFRACTION Dmax: 74.2 Å Quality: EXCELLENT

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

50S ribosomal protein L1

Thermus thermophilus

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–68 Chain A; UniProt 160–229 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;277 K;30% v/v polyethylenglycol 4K, 100 mM Tris-HCl, 200 mM LiSO4, pH 8.5, VAPOR DIFFUSION, temperature 277K Resolution 2.30 Å R-free 0.233
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–68 Chain B; UniProt 160–229 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;277 K;30% v/v polyethylenglycol 4K, 100 mM Tris-HCl, 200 mM LiSO4, pH 8.5, VAPOR DIFFUSION, temperature 277K Resolution 2.30 Å R-free 0.233
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 2–68 Chain C; UniProt 160–229 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;277 K;30% v/v polyethylenglycol 4K, 100 mM Tris-HCl, 200 mM LiSO4, pH 8.5, VAPOR DIFFUSION, temperature 277K Resolution 2.30 Å R-free 0.233

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 53 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 A; PDBConstruct 1–67; UniProt 2–68 Author chain A; PDBConstruct 68–137; UniProt 160–229 Author chain B; PDBConstruct 1–67; UniProt 2–68 Author chain B; PDBConstruct 68–137; UniProt 160–229 Author chain C; PDBConstruct 1–67; UniProt 2–68 Author chain C; PDBConstruct 68–137; UniProt 160–229

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 2ov7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ov7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ov7
Deposition date deposition_date2007-02-13
Structure title titleThe first domain of the ribosomal protein L1 from Thermus thermophilus
Keywords keywordsribosomal protein L1, Thermus thermophilus, RIBOSOMAL PROTEIN; RIBOSOMAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.15
Radius of gyration Rg (electron density) rg_electron23.01
Forward intensity I(0) i032779700.00
Molecular weight molecular_weight43563.0 kDa
Excluded volume excluded_volume54604 ų
Envelope volume envelope_volume71296 ų
Hydration-shell volume shell_volume25911 ų
Envelope diameter envelope_diameter75.3
Shell Rg shell_rg29.84
Envelope Rg envelope_rg22.89
Shape Rg shape_rg22.99
Total Rg total_rg23.94
Total atoms total_atoms3076
Residues n_residues395
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 dmax74.2
Rg (real space) rg_real24.01
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real3.2780e+07
I(0) uncertainty (real space) i0_real_error4.6110e+05
Rg (reciprocal space) rg_reciprocal24.05
I(0) (reciprocal space) i0_reciprocal32780000.0000
Solution quality estimate total_estimate0.9105
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.5
Skewness Skewness skewness0.141
Kurtosis Kurtosis kurtosis-0.541
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12000000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id2ov7A01
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology20 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily140 — 50S ribosomal protein L1; Chain A, Domain 1
Domain ID domain_id2ov7B01
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology20 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily140 — 50S ribosomal protein L1; Chain A, Domain 1
Domain ID domain_id2ov7C01
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology20 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily140 — 50S ribosomal protein L1; Chain A, Domain 1

8. Citations (1)

9. Files and Curves (10)