3fl0

X-ray structure of the non covalent swapped form of the Q28L/K31C/S32C mutant of bovine pancreatic ribonuclease in complex with 2'-DEOXYCYTIDINE-2'-DEOXYGUANOSINE-3',5'-MONOPHOSPHATE

Method: X-RAY DIFFRACTION Dmax: 72.7 Å Quality: GOOD

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

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–150 Chain B; UniProt 27–150 Mutation:Q28L, K31C, S32C Non-standard monomer:Yes (specific site not provided by mmCIF) CGP 2'-DEOXYCYTIDINE-2'-DEOXYGUANOSINE-3',5'-MONOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;21% PEG 35000, 0.2M sodium acetate, 0.1M Tris/HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.94 Å R-free 0.227

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 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 3fl0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3fl0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3fl0
Deposition date deposition_date2008-12-18
Structure title titleX-ray structure of the non covalent swapped form of the Q28L/K31C/S32C mutant of bovine pancreatic ribonuclease in complex with 2'-DEOXYCYTIDINE-2'-DEOXYGUANOSINE-3',5'-MONOPHOSPHATE
Keywords keywords;3D-domain swapping, bovine seminal ribonuclease, non-covalent dimer, antitumor activity, quaternary structure flexibility, protein mutations and evolution, Endonuclease, Glycation, Glycoprotein, Hydrolase, Nuclease, Secreted ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.54
Radius of gyration Rg (electron density) rg_electron22.08
Forward intensity I(0) i016243800.00
Molecular weight molecular_weight27632.0 kDa
Excluded volume excluded_volume33367 ų
Envelope volume envelope_volume41784 ų
Hydration-shell volume shell_volume16634 ų
Envelope diameter envelope_diameter74.6
Shell Rg shell_rg27.21
Envelope Rg envelope_rg22.08
Shape Rg shape_rg22.09
Total Rg total_rg22.72
Total atoms total_atoms1913
Residues n_residues241
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 dmax72.7
Rg (real space) rg_real22.59
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real1.6240e+07
I(0) uncertainty (real space) i0_real_error2.0420e+05
Rg (reciprocal space) rg_reciprocal22.58
I(0) (reciprocal space) i0_reciprocal16240000.0000
Solution quality estimate total_estimate0.8966
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.8
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.629
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2598000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.903; Smooth: 0.990

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_idd3fl0a_
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_idd3fl0b_
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_id3fl0A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain
Domain ID domain_id3fl0B00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain

8. Citations (4)

9. Files and Curves (10)