2vpl

The structure of the complex between the first domain of L1 protein from Thermus thermophilus and mRNA from Methanococcus jannaschii

Method: X-RAY DIFFRACTION Dmax: 90.4 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–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain A; UniProt 2–68 Chain A; UniProt 160–229 Fragment:FIRST DOMAIN, RESIDUES 2-68,160-229 FRAGMENT OF MRNA FOR L1-OPERON CONTAINING REGULATOR L1-BINDING SITE × 1 K POTASSIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å R-free 0.274
2 Protein–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain C; UniProt 2–68 Chain C; UniProt 160–229 Fragment:FIRST DOMAIN, RESIDUES 2-68,160-229 FRAGMENT OF MRNA FOR L1-OPERON CONTAINING REGULATOR L1-BINDING SITE × 1 K POTASSIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å R-free 0.274

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 54 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 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 2vpl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2vpl
Deposition date deposition_date2008-03-01
Structure title titleThe structure of the complex between the first domain of L1 protein from Thermus thermophilus and mRNA from Methanococcus jannaschii
Keywords keywordsRIBOSOMAL PROTEIN, RNA-PROTEIN COMPLEX, TRANSLATION REGULATION, TRANSLATION, REPRESSOR, RNA-BINDING, TRNA-BINDING, RRNA-BINDING; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.12
Radius of gyration Rg (electron density) rg_electron28.45
Forward intensity I(0) i0111508000.00
Molecular weight molecular_weight60970.0 kDa
Excluded volume excluded_volume66596 ų
Envelope volume envelope_volume98812 ų
Hydration-shell volume shell_volume29123 ų
Envelope diameter envelope_diameter96.5
Shell Rg shell_rg35.59
Envelope Rg envelope_rg28.02
Shape Rg shape_rg28.48
Total Rg total_rg28.94
Total atoms total_atoms4162
Residues n_residues368
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 dmax90.4
Rg (real space) rg_real28.12
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.1150e+08
I(0) uncertainty (real space) i0_real_error1.7670e+06
Rg (reciprocal space) rg_reciprocal28.13
I(0) (reciprocal space) i0_reciprocal111500000.0000
Solution quality estimate total_estimate0.9017
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.9
Skewness Skewness skewness0.316
Kurtosis Kurtosis kurtosis-0.378
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8690000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.935

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id2vplA01
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_id2vplC01
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)