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Crystal Structure of The Swapped non covalent form of P19A/L28Q/N67D BS-RNase

Analyse Crystal Structure of The Swapped non covalent form of P19A/L28Q/N67D BS-RNase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3BCP
Type
protein
Length
496 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.57
Source
Bos taurus
Molecule
Seminal ribonuclease
EC
3.1.27.5
UniProt
P00669
Pockets
6 · best druggability 0.84

Structure

x-ray diffraction · resolution 2.57 · 1 distinct chain · 19% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DSeminal ribonuclease (EC 3.1.27.5)protein12419% helix, 35% strandP00669

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111200.840.85118empty
22240.620.8232empty
33090.610.7935empty
4550.430.8316empty
51040.400.7620empty

Interfaces

6 interfaces between chains.

  • A–B · 1743 Ų buried · 37 hydrogen bonds · protein-protein
  • C–D · 1735 Ų buried · 37 hydrogen bonds · protein-protein
  • B–D · 844 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 732 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 272 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide, 8 modified (disulfide, alkylation).

Compared structures

  • 3BCP · Crystal structure of the swapped non covalent form of P19A/L28Q/N67D bs-RNase · the same entry in another collection · chain A against A, TM-score 1.00
  • P00669 · AlphaFold monomer V2.0 prediction for seminal ribonuclease (P00669) · a predicted model of the same protein · chain A against A, TM-score 0.82

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