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The domain-swapped dimer of cv-N in solution

Analyse The domain-swapped dimer of cv-N in solution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1L5E
Type
protein
Length
202 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cyanovirin-N
UniProt
P81180
Pockets
2 · best druggability 0.31

Structure

solution nmr · 1 distinct chain · 7% helix, 57% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCyanovirin-Nprotein1017% helix, 57% strandP81180

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1710.310.7418empty
2520.280.7516empty

Interfaces

1 interface between chains.

  • A–B · 3392 Ų buried · 63 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 1L5E · The domain-swapped dimer of CV-N in solution · the same entry in another collection · chain A against A, TM-score 1.00
  • P81180 · AlphaFold monomer V2.0 prediction for cyanovirin-N (P81180) · a predicted model of the same protein · chain A against A, TM-score 0.49

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