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NMR structure of the heterodimeric complex between cad domains of cad and icad

Analyse NMR structure of the heterodimeric complex between cad domains of cad and icad in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1F2R
Type
protein
Length
187 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Caspase-activated DNase; Inhibitor of caspase-activated DNase
UniProt
O54788, O54786
Pockets
1 · best druggability 0.31

Structure

solution nmr · 2 distinct chains · 14% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CCaspase-activated DNaseprotein8714% helix, 28% strandO54788
IInhibitor of caspase-activated DNaseprotein10015% helix, 26% strandO54786

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1520.310.7717empty

Interfaces

1 interface between chains.

  • C–I · 596 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 1F2R · NMR structure of the heterodimeric complex between cad domains of cad and icad · the same entry in another collection · chain C against C, TM-score 1.00
  • O54788 · AlphaFold monomer V2.0 prediction for DNA fragmentation factor subunit beta (O54788) · a predicted model of the same protein · chain C against A, TM-score 0.75
  • O54786 · AlphaFold monomer V2.0 prediction for DNA fragmentation factor subunit alpha (O54786) · a predicted model of the same protein · chain I against A, TM-score 0.74

Analyse

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