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X-ray-crystallographic structure of an RNase PO1 exhibiting anti-tumor activity

Analyse X-ray-crystallographic structure of an RNase PO1 exhibiting anti-tumor activity in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3WHO
Type
protein
Length
303 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Guanyl-specific ribonuclease PO1
EC
3.1.27.3
UniProt
P81762

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CGuanyl-specific ribonuclease PO1 (EC 3.1.27.3)protein10112% helix, 35% strandP81762

Interfaces

2 interfaces between chains.

  • A–C · 335 Ų buried · 4 hydrogen bonds · protein-protein
  • A–B · 309 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

  • 3WHO · X-ray-Crystallographic Structure of an RNase Po1 Exhibiting Anti-tumor Activity · the same entry in another collection · chain C against C, TM-score 1.00
  • P81762 · AlphaFold monomer V2.0 prediction for guanyl-specific ribonuclease PO1 (P81762) · a predicted model of the same protein · chain A against A, TM-score 0.96

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