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Re-engineering topology of the homodimeric rop protein into a single- chain 4-helix bundle

Analyse Re-engineering topology of the homodimeric rop protein into a single- chain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1YO7
Type
protein
Length
240 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Regulatory protein rop
UniProt
P03051
Ligands
ZN
Pockets
2 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 87% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BRegulatory protein ropprotein12087% helix, 0% strandP03051

Ligands and binding sites

  • ZN · Zinc ion · metal · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1680.340.7611empty
2580.310.7611empty

Interfaces

1 interface between chains.

  • A–B · 743 Ų buried · 27 hydrogen bonds · protein-protein

Compared structures

  • 1YO7 · Re-engineering topology of the homodimeric ROP protein into a single-chain 4-helix bundle · the same entry in another collection · chain A against A, TM-score 1.00
  • P03051 · AlphaFold monomer V2.0 prediction for regulatory protein rop (P03051) · a predicted model of the same protein · chain A against A, TM-score 0.47

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