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Engineering domain-swapped binding interfaces by mutually exclusive folding: insertion of ubiquitin into position 103 of barnase

Analyse Engineering domain-swapped binding interfaces by mutually exclusive folding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3Q3F
Type
protein
Length
188 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RIBONUCLEASE/UBIQUITIN chimeric protein
UniProt
P00648, P0CG48
Ligands
SO4
Pockets
1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARIBONUCLEASE/UBIQUITIN chimeric proteinprotein18822% helix, 24% strandP00648, P0CG48

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 16 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12610.650.8238SO4

Compared structures

  • 3Q3F · Engineering Domain-Swapped Binding Interfaces by Mutually Exclusive Folding: Insertion of… · the same entry in another collection · chain A against A, TM-score 1.00

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