4f9t

Ribosomal protein L1 from Thermus thermophilus with substitution Thr217Ala

Method: X-RAY DIFFRACTION Dmax: 60.9 Å Quality: EXCELLENT

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–229 Mutation:T217A MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 3 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 1 SO4 SULFATE ION × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 10;295 K;15 MG/ML L1 50 MM GLYCINE,INITIALLY AT PH 10 5% (V/V)METHANE PENTANEDIOL 1.2 M AMMONIUM SULFATE EQUILIBRATED AGAINST 2.4 M AMMONIUM SULFATE 7% (V/V) METHANE PENTANEDIOL , VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.46 Å R-free 0.202

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 A; PDBConstruct 1–229; UniProt 1–229

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 4f9t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4f9t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4f9t
Deposition date deposition_date2012-05-21
Structure title titleRibosomal protein L1 from Thermus thermophilus with substitution Thr217Ala
Keywords keywordsRossmann fold, Ribosomal protein, RNA; RIBOSOMAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.48
Radius of gyration Rg (electron density) rg_electron18.23
Forward intensity I(0) i012769000.00
Molecular weight molecular_weight25817.0 kDa
Excluded volume excluded_volume32069 ų
Envelope volume envelope_volume38274 ų
Hydration-shell volume shell_volume17760 ų
Envelope diameter envelope_diameter61.9
Shell Rg shell_rg24.22
Envelope Rg envelope_rg18.41
Shape Rg shape_rg18.21
Total Rg total_rg19.20
Total atoms total_atoms1802
Residues n_residues226
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 dmax60.9
Rg (real space) rg_real19.37
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real1.2770e+07
I(0) uncertainty (real space) i0_real_error1.7490e+05
Rg (reciprocal space) rg_reciprocal19.39
I(0) (reciprocal space) i0_reciprocal12770000.0000
Solution quality estimate total_estimate0.9025
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.0
Skewness Skewness skewness0.172
Kurtosis Kurtosis kurtosis-0.475
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3154000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.969

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4f9tA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology190 — Ribulose 1,5 Bisphosphate Carboxylase/Oxygenase
Homologous superfamily homologous superfamily20 — Ribosomal protein L1/L10, rRNA-binding domain
Domain ID domain_id4f9tA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily790 — Ribosomal protein L1/L10, domain II

8. Citations (1)

9. Files and Curves (10)