3mwr

Crystal structure of ribonuclease A tandem enzymes and their interaction with the cytosolic ribonuclease inhibitor

Method: X-RAY DIFFRACTION Dmax: 75.7 Å Quality: GOOD

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

Ribonuclease pancreatic, LINKER, Ribonuclease pancreatic

Bos taurus

UniProt P61823

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 27–150 Chain A; UniProt 27–150 Not recorded SO4 SULFATE ION × 4 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.9;286 K;30% PEG 8000, 0.2M ammonium sulfate, pH 5.9, VAPOR DIFFUSION, HANGING DROP, temperature 286K Resolution 1.85 Å R-free 0.207

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.

333 other PDB entries and 495 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNAS1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–124; UniProt 27–150 Author chain A; PDBConstruct 131–254; UniProt 27–150

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 3mwr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3mwr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3mwr
Deposition date deposition_date2010-05-06
Structure title titleCrystal structure of ribonuclease A tandem enzymes and their interaction with the cytosolic ribonuclease inhibitor
Keywords keywordsribonuclease A tandem enzyme, SGSGSG-linker, Hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.54
Radius of gyration Rg (electron density) rg_electron21.09
Forward intensity I(0) i017419600.00
Molecular weight molecular_weight28135.0 kDa
Excluded volume excluded_volume33810 ų
Envelope volume envelope_volume42153 ų
Hydration-shell volume shell_volume17855 ų
Envelope diameter envelope_diameter77.1
Shell Rg shell_rg26.04
Envelope Rg envelope_rg21.29
Shape Rg shape_rg21.07
Total Rg total_rg21.78
Total atoms total_atoms1947
Residues n_residues252
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 dmax75.7
Rg (real space) rg_real21.66
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real1.7420e+07
I(0) uncertainty (real space) i0_real_error2.6230e+05
Rg (reciprocal space) rg_reciprocal21.64
I(0) (reciprocal space) i0_reciprocal17420000.0000
Solution quality estimate total_estimate0.8512
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.484
Kurtosis Kurtosis kurtosis-0.225
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3459000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.758; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.798; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3mwrA01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain
Domain ID domain_id3mwrA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain

8. Citations (1)

9. Files and Curves (10)