1ssc

THE 1.6 ANGSTROMS STRUCTURE OF A SEMISYNTHETIC RIBONUCLEASE CRYSTALLIZED FROM AQUEOUS ETHANOL. COMPARISON WITH CRYSTALS FROM SALT SOLUTIONS AND WITH RNASE A FROM AQUEOUS ALCOHOL SOLUTIONS

Method: X-RAY DIFFRACTION Dmax: 51.4 Å Quality: GOOD

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

RIBONUCLEASE A

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–138 Chain B; UniProt 140–150 Not recorded PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å

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, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–112; UniProt 27–138 Author chain B; PDBConstruct 1–11; UniProt 140–150

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 1ssc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ssc
Deposition date deposition_date1994-10-05
Structure title titleTHE 1.6 ANGSTROMS STRUCTURE OF A SEMISYNTHETIC RIBONUCLEASE CRYSTALLIZED FROM AQUEOUS ETHANOL. COMPARISON WITH CRYSTALS FROM SALT SOLUTIONS AND WITH RNASE A FROM AQUEOUS ALCOHOL SOLUTIONS
Keywords keywordsENDONUCLEASE; ENDONUCLEASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.05
Radius of gyration Rg (electron density) rg_electron14.18
Forward intensity I(0) i04463220.00
Molecular weight molecular_weight13676.0 kDa
Excluded volume excluded_volume16515 ų
Envelope volume envelope_volume18924 ų
Hydration-shell volume shell_volume11556 ų
Envelope diameter envelope_diameter49.7
Shell Rg shell_rg19.58
Envelope Rg envelope_rg14.49
Shape Rg shape_rg14.18
Total Rg total_rg15.19
Total atoms total_atoms948
Residues n_residues123
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 dmax51.4
Rg (real space) rg_real15.00
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real4.4630e+06
I(0) uncertainty (real space) i0_real_error5.1500e+04
Rg (reciprocal space) rg_reciprocal15.00
I(0) (reciprocal space) i0_reciprocal4463000.0000
Solution quality estimate total_estimate0.8761
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.1
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.388
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha967400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 1.000

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_idd1ssc.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_id1sscA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain

8. Citations (3)

9. Files and Curves (10)