1r3m

Crystal structure of the dimeric unswapped form of bovine seminal ribonuclease

Method: X-RAY DIFFRACTION Dmax: 74.1 Å Quality: GOOD

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

Ribonuclease, seminal

OrganismNot specified

UniProt P00669

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 Not recorded PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.4;294 K;MPD, ammonium sulfate, pH 8.4, EVAPORATION, temperature 294K Resolution 2.20 Å R-free 0.292
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 27–150 Not recorded PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.4;294 K;MPD, ammonium sulfate, pH 8.4, EVAPORATION, temperature 294K Resolution 2.20 Å R-free 0.292

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.

20 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNS_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–124; UniProt 27–150 Author chain B; PDBConstruct 1–124; 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 1r3m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1r3m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1r3m
Deposition date deposition_date2003-10-02
Structure title titleCrystal structure of the dimeric unswapped form of bovine seminal ribonuclease
Keywords keywordsRIBONUCLEASE, SWAPPING, HINGE, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.23
Radius of gyration Rg (electron density) rg_electron21.15
Forward intensity I(0) i015421300.00
Molecular weight molecular_weight27081.0 kDa
Excluded volume excluded_volume32903 ų
Envelope volume envelope_volume40169 ų
Hydration-shell volume shell_volume17057 ų
Envelope diameter envelope_diameter74.7
Shell Rg shell_rg26.38
Envelope Rg envelope_rg21.30
Shape Rg shape_rg21.16
Total Rg total_rg21.83
Total atoms total_atoms1868
Residues n_residues244
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 dmax74.1
Rg (real space) rg_real21.42
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real1.5420e+07
I(0) uncertainty (real space) i0_real_error2.2750e+05
Rg (reciprocal space) rg_reciprocal21.39
I(0) (reciprocal space) i0_reciprocal15420000.0000
Solution quality estimate total_estimate0.7624
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.8
Skewness Skewness skewness0.574
Kurtosis Kurtosis kurtosis-0.107
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2513000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.716; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.760; Smooth: 0.000

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_idd1r3ma_
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
Domain ID domain_idd1r3mb_
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 (2 domains)

Domain ID domain_id1r3mA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain
Domain ID domain_id1r3mB00
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)