1uci

Mutants of RNase Sa

Method: X-RAY DIFFRACTION Dmax: 72.4 Å Quality: GOOD

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

Guanyl-specific ribonuclease Sa

Streptomyces aureofaciens

UniProt P05798

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 1–96 Mutation:V2T SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;1.6M ammonium sulfate, 0.1M MES pH 6.5, 10%(v/v) dioxane, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.80 Å R-free 0.208
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–96 Mutation:V2T No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;1.6M ammonium sulfate, 0.1M MES pH 6.5, 10%(v/v) dioxane, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.80 Å R-free 0.208

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.

27 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNSA_STRAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–96; UniProt 1–96 Author chain B; PDBConstruct 1–96; UniProt 1–96

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 1uci

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1uci
Deposition date deposition_date2003-04-15
Structure title titleMutants of RNase Sa
Keywords keywordsProtein Stability, Hydrogen Bond, Burial Polar, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.36
Radius of gyration Rg (electron density) rg_electron20.77
Forward intensity I(0) i08974550.00
Molecular weight molecular_weight21237.0 kDa
Excluded volume excluded_volume26086 ų
Envelope volume envelope_volume32241 ų
Hydration-shell volume shell_volume14219 ų
Envelope diameter envelope_diameter70.2
Shell Rg shell_rg24.99
Envelope Rg envelope_rg20.81
Shape Rg shape_rg20.73
Total Rg total_rg21.53
Total atoms total_atoms1497
Residues n_residues192
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 dmax72.4
Rg (real space) rg_real21.54
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real8.9750e+06
I(0) uncertainty (real space) i0_real_error1.2050e+05
Rg (reciprocal space) rg_reciprocal21.50
I(0) (reciprocal space) i0_reciprocal8974000.0000
Solution quality estimate total_estimate0.8149
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.2
Skewness Skewness skewness0.463
Kurtosis Kurtosis kurtosis-0.551
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3491000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.642; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.669; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ucia_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.1 — Microbial ribonucleases
Superfamily Superfamily superfamilyd.1.1 — Microbial ribonucleases
Family Family familyd.1.1.2 — Bacterial ribonucleases
Domain ID domain_idd1ucib_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.1 — Microbial ribonucleases
Superfamily Superfamily superfamilyd.1.1 — Microbial ribonucleases
Family Family familyd.1.1.2 — Bacterial ribonucleases

CATH v4.4 (2 domains)

Domain ID domain_id1uciA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily30 — Microbial ribonucleases
Domain ID domain_id1uciB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily30 — Microbial ribonucleases

8. Citations (1)

9. Files and Curves (10)