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Fungal antifreeze protein exerts hyperactivity by constructing an inequable beta-helix

Analyse Fungal antifreeze protein exerts hyperactivity by constructing an inequable… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3VN3
Type
protein
Length
446 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Antifreeze protein
UniProt
Q76CE6
Pockets
1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAntifreeze proteinprotein22316% helix, 42% strandQ76CE6

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 7 copies · chains A, B

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
13990.540.7341EDO

Interfaces

1 interface between chains.

  • A–B · 54 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nonstandard).

Compared structures

  • 3VN3 · Fungal antifreeze protein exerts hyperactivity by constructing an inequable beta-helix · the same entry in another collection · chain A against A, TM-score 1.00
  • Q76CE6 · AlphaFold monomer V2.0 prediction for ice-binding protein K3-B1 (Q76CE6) · a predicted model of the same protein · chain A against A, TM-score 1.00

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