7vb2

Solution structure of human ribosomal protein uL11

Method: SOLUTION NMR Dmax: 99.3 Å Quality: REASONABLE

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

60S ribosomal protein L12

Homo sapiens

UniProt P30050

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 1–165 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;306 K;Ionic strength (raw mmCIF value) 20mM sodium phosphate,50mM sodium sulfate;Pressure 1 NMR sample composition:0.3 mM [U-15N] human uL11, 20 mM sodium phosphate, 50 mM sodium sulfate, 0.3 % w/v CHAPS, 5 mM DTT, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.3 mM [U-13C; U-15N] human uL11, 20 mM sodium phosphate, 50 mM sodium sulfate, 0.3 % w/v CHAPS, 5 mM DTT, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.3 mM human uL11, 20 mM sodium phosphate, 50 mM sodium sulfate, 0.3 % w/v CHAPS, 5 mM DTT, 95% H2O/5% D2O | 95% H2O/5% D2O Resolution not provided

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.

89 other PDB entries and 89 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL12_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–165; UniProt 1–165

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 7vb2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7vb2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7vb2
Deposition date deposition_date2021-08-30
Structure title titleSolution structure of human ribosomal protein uL11
Keywords keywordsribosomal protein, translation, elongation factors; RIBOSOMAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier39.35
Radius of gyration Rg (electron density) rg_electron40.76
Forward intensity I(0) i0471304000.00
Molecular weight molecular_weight178260.0 kDa
Excluded volume excluded_volume223470 ų
Envelope volume envelope_volume247030 ų
Hydration-shell volume shell_volume47774 ų
Envelope diameter envelope_diameter175.0
Shell Rg shell_rg44.45
Envelope Rg envelope_rg48.99
Shape Rg shape_rg40.74
Total Rg total_rg40.97
Total atoms total_atoms25550
Residues n_residues1650
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 dmax99.3
Rg (real space) rg_real36.71
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real4.4630e+08
I(0) uncertainty (real space) i0_real_error5.7730e+06
Rg (reciprocal space) rg_reciprocal39.64
I(0) (reciprocal space) i0_reciprocal471100000.0000
Solution quality estimate total_estimate0.5974
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.3
Skewness Skewness skewness0.174
Kurtosis Kurtosis kurtosis-1.081
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha1.7020
Highest regularization parameter α highest_alpha606000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.887; Stabil: 0.927; Sysdev: 0.000; Positv: 1.000; Valcen: 0.329; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7vb2A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1550 — Ribosomal protein L11, N-terminal domain
Homologous superfamily homologous superfamily10 — Ribosomal protein L11/L12, N-terminal domain

8. Citations (1)

9. Files and Curves (10)