1bxy

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L30 FROM THERMUS THERMOPHILUS AT 1.9 A RESOLUTION: CONFORMATIONAL FLEXIBILITY OF THE MOLECULE.

Method: X-RAY DIFFRACTION Dmax: 67.7 Å Quality: GOOD

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

PROTEIN (RIBOSOMAL PROTEIN L30)

Thermus thermophilus

UniProt P74909

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 1–60 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;pH 7.5 Resolution 1.90 Å R-free 0.253
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–60 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;pH 7.5 Resolution 1.90 Å R-free 0.253

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.

16 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL30_THETH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–60; UniProt 1–60 Author chain B; PDBConstruct 1–60; UniProt 1–60

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 1bxy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bxy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bxy
Deposition date deposition_date1998-10-09
Structure title titleCRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L30 FROM THERMUS THERMOPHILUS AT 1.9 A RESOLUTION: CONFORMATIONAL FLEXIBILITY OF THE MOLECULE.
Keywords keywordsRIBOSOMAL PROTEIN, CONFORMATIONAL CHANGES, RIBOSOME; RIBOSOME
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.14
Radius of gyration Rg (electron density) rg_electron19.81
Forward intensity I(0) i03189700.00
Molecular weight molecular_weight13548.0 kDa
Excluded volume excluded_volume17377 ų
Envelope volume envelope_volume22125 ų
Hydration-shell volume shell_volume10267 ų
Envelope diameter envelope_diameter65.8
Shell Rg shell_rg23.73
Envelope Rg envelope_rg19.50
Shape Rg shape_rg19.79
Total Rg total_rg20.55
Total atoms total_atoms952
Residues n_residues120
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 dmax67.7
Rg (real space) rg_real20.29
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real3.1900e+06
I(0) uncertainty (real space) i0_real_error4.8180e+04
Rg (reciprocal space) rg_reciprocal20.27
I(0) (reciprocal space) i0_reciprocal3190000.0000
Solution quality estimate total_estimate0.7695
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.5
Skewness Skewness skewness0.384
Kurtosis Kurtosis kurtosis-0.700
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha968900.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.521; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.573; Smooth: 0.862

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1bxya_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.59 — Ribosomal protein L30p/L7e
Superfamily Superfamily superfamilyd.59.1 — Ribosomal protein L30p/L7e
Family Family familyd.59.1.1 — Ribosomal protein L30p/L7e
Domain ID domain_idd1bxyb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.59 — Ribosomal protein L30p/L7e
Superfamily Superfamily superfamilyd.59.1 — Ribosomal protein L30p/L7e
Family Family familyd.59.1.1 — Ribosomal protein L30p/L7e

CATH v4.4 (2 domains)

Domain ID domain_id1bxyA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1390 — Ribosomal Protein L30; Chain: A,
Homologous superfamily homologous superfamily20 — Ribosomal protein L30/L7
Domain ID domain_id1bxyB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1390 — Ribosomal Protein L30; Chain: A,
Homologous superfamily homologous superfamily20 — Ribosomal protein L30/L7

8. Citations (1)

9. Files and Curves (10)