1z3p

X-Ray crystal structure of a mutant Ribonuclease S (M13Nva)

Method: X-RAY DIFFRACTION Dmax: 51.8 Å Quality: GOOD

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

Ribonuclease pancreatic, S-Peptide

OrganismNot specified

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 47–150 Chain S; UniProt 27–41 Mutation:M13NVA Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:Batch method;pH 5.2;293 K;ammonium sulfate, cesium chloride, sodium acetate, pH 5.2, Batch method, temperature 293K Resolution 2.00 Å R-free 0.233

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 RNP_BOVIN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain S; PDBConstruct 1–15; UniProt 27–41 Author chain E; PDBConstruct 1–104; UniProt 47–150

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 1z3p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1z3p
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1z3p
Deposition date deposition_date2005-03-14
Structure title titleX-Ray crystal structure of a mutant Ribonuclease S (M13Nva)
Keywords keywordsRNase S mutant (M13Nva), S-Peptide, S-Protein, cavity, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.38
Radius of gyration Rg (electron density) rg_electron14.46
Forward intensity I(0) i04357490.00
Molecular weight molecular_weight13456.0 kDa
Excluded volume excluded_volume16217 ų
Envelope volume envelope_volume18680 ų
Hydration-shell volume shell_volume11341 ų
Envelope diameter envelope_diameter49.2
Shell Rg shell_rg19.80
Envelope Rg envelope_rg14.71
Shape Rg shape_rg14.46
Total Rg total_rg15.46
Total atoms total_atoms932
Residues n_residues118
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 dmax51.8
Rg (real space) rg_real15.35
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real4.3570e+06
I(0) uncertainty (real space) i0_real_error4.7250e+04
Rg (reciprocal space) rg_reciprocal15.36
I(0) (reciprocal space) i0_reciprocal4357000.0000
Solution quality estimate total_estimate0.8849
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.0
Skewness Skewness skewness0.271
Kurtosis Kurtosis kurtosis-0.382
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha801600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1z3p.1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.5 — RNase A-like
Superfamily Superfamily superfamilyd.5.1 — RNase A-like
Family Family familyd.5.1.1 — Ribonuclease A-like

CATH v4.4 (1 domains)

Domain ID domain_id1z3pE00
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)