9xb4

Crystal structure of Mrt4 (L96C) mutant

Method: X-RAY DIFFRACTION Dmax: 79.2 Å Quality: GOOD

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

Large ribosomal subunit protein uL10

Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

UniProt G0S616

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 1–270 Mutation:L96C Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;291 K;0.1 M bicine and 2.22 M (NH4)2SO4 Resolution 2.50 Å R-free 0.283

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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MRT4_CHATD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–270; UniProt 1–270

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 9xb4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9xb4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9xb4
Deposition date deposition_date2025-10-23
最后修订 last_revision2026-02-04
Structure title titleCrystal structure of Mrt4 (L96C) mutant
Keywords keywords;Fumaramidmycin-based derivatives, Azole-resistant fungi, ribosome assembly factor, target identification, protein-RNA interaction, RNA BINDING PROTEIN ;; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.30
Radius of gyration Rg (electron density) rg_electron22.93
Forward intensity I(0) i011374000.00
Molecular weight molecular_weight24781.0 kDa
Excluded volume excluded_volume30749 ų
Envelope volume envelope_volume38715 ų
Hydration-shell volume shell_volume15637 ų
Envelope diameter envelope_diameter81.0
Shell Rg shell_rg27.35
Envelope Rg envelope_rg22.93
Shape Rg shape_rg22.90
Total Rg total_rg23.63
Total atoms total_atoms1727
Residues n_residues214
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 dmax79.2
Rg (real space) rg_real23.57
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real1.1370e+07
I(0) uncertainty (real space) i0_real_error1.6170e+05
Rg (reciprocal space) rg_reciprocal23.51
I(0) (reciprocal space) i0_reciprocal11370000.0000
Solution quality estimate total_estimate0.8041
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.5
Skewness Skewness skewness0.527
Kurtosis Kurtosis kurtosis-0.502
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2405000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.639; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.579; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)