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- PDB-3bco: Crystal Structure of The Swapped FOrm of P19A/L28Q/N67D BS-RNase -

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Database: PDB / ID: 3bco
TitleCrystal Structure of The Swapped FOrm of P19A/L28Q/N67D BS-RNase
ComponentsSeminal ribonuclease
KeywordsHYDROLASE / domain swapping / bovine seminal ribonuclease / non covalent dimer / antitumor activity / Allosteric enzyme / Endonuclease / Secreted
Function / homology
Function and homology information

pancreatic ribonuclease / ribonuclease A activity / RNA phosphodiester bond hydrolysis / ribonuclease activity / nucleic acid binding / lyase activity / extracellular region / identical protein binding
Similarity search - Function
P-30 Protein / Ribonuclease A-like domain / Pancreatic ribonuclease family signature. / Ribonuclease A-domain / Pancreatic ribonuclease / Pancreatic ribonuclease / Ribonuclease A-like domain superfamily / Pancreatic ribonuclease / Ribonuclease A, active site / Roll / Alpha Beta
Similarity search - Domain/homology
Seminal ribonuclease
Similarity search - Component
Biological speciesBos taurus (cattle)
AuthorsMerlino, A. / Ercole, C. / Picone, D. / Pizzo, E. / Mazzarella, L. / Sica, F.
Journal: J.Mol.Biol. / Year: 2008
Title: The buried diversity of bovine seminal ribonuclease: shape and cytotoxicity of the swapped non-covalent form of the enzyme
Authors: Merlino, A. / Ercole, C. / Picone, D. / Pizzo, E. / Mazzarella, L. / Sica, F.
#1: Journal: J.Biol.Chem. / Year: 2004
Title: Structure and stability of the non-covalent swapped dimer of bovine seminal ribonuclease: an enzyme tailored to evade ribonuclease protein inhibitor
Authors: Sica, F. / Di Fiore, A. / Merlino, A. / Mazzarella, L.
#2: Journal: Biopolymers / Year: 2004
Title: Population shift vs induced fit: the case of bovine seminal ribonuclease swapping dimer
Authors: Merlino, A. / Vitagliano, L. / Sica, F. / Zagari, A. / Mazzarella, L.
#3: Journal: Acta Crystallogr.,Sect.D / Year: 1993
Title: Bovine seminal ribonuclease: structure at 1.9 A resolution
Authors: Mazzarella, L. / Capasso, S. / Demasi, D. / Di Lorenzo, G. / Mattia, C.A. / Zagari, A.
#4: Journal: Proteins / Year: 2003
Title: The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative
Authors: Sica, F. / Di Fiore, A. / Zagari, A. / Mazzarella, L.
#5: Journal: J.Mol.Biol. / Year: 1999
Title: A potential allosteric subsite generated by domain swapping in bovine seminal ribonuclease
Authors: Vitagliano, L. / Adinolfi, S. / Sica, F. / Merlino, A. / Zagari, A. / Mazzarella, L.
#6: Journal: Protein Sci. / Year: 1998
Title: Binding of a substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2',5')adenosine
Authors: Vitagliano, L. / Adinolfi, S. / Riccio, A. / Sica, F. / Zagari, A. / Mazzarella, L.
DepositionNov 13, 2007Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Feb 12, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 10, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

Structure visualization

Structure viewerMolecule:

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Deposited unit
A: Seminal ribonuclease
B: Seminal ribonuclease

Theoretical massNumber of molelcules
Total (without water)27,2452

  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3690 Å2
Unit cell
Length a, b, c (Å)48.551, 62.305, 81.143
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121


#1: Protein Seminal ribonuclease / Seminal RNase / S-RNase / Ribonuclease BS-1

Mass: 13622.559 Da / Num. of mol.: 2 / Mutation: P19A, L28Q, N67D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / Gene: SRN / Plasmid: PET-22B(+) / Production host: Escherichia coli (E. coli) / References: UniProt: P00669, EC:
#2: Water ChemComp-HOH / water / Water

Mass: 18.015 Da / Num. of mol.: 87 / Source method: isolated from a natural source / Formula: H2O

Experimental details


ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

Sample preparation

CrystalDensity Matthews: 2.25 Å3/Da / Density % sol: 45.39 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 28% w/v PEG 8000, 0.2M SODIUM ACETATE, 0.1M CACODILATE pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å
DetectorType: ENRAF-NONIUS / Detector: AREA DETECTOR / Date: Mar 22, 2004 / Details: mirrors
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.2→20 Å / Num. obs: 12492 / % possible obs: 93.4 % / Observed criterion σ(I): 0 / Redundancy: 4 % / Rmerge(I) obs: 0.041 / Net I/σ(I): 17.9
Reflection shellResolution: 2.2→2.24 Å / Redundancy: 4 % / Rmerge(I) obs: 0.247 / Mean I/σ(I) obs: 5 / % possible all: 93.5


HKL-2000data collection
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1R5D
Resolution: 2.25→20 Å / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.25 1150 RANDOM
Rwork0.218 --
obs0.218 10017 -
Refinement stepCycle: LAST / Resolution: 2.25→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1880 0 0 87 1967
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.007
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.4
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d25.2
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d0.8
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot

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