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Disulphide linked homodimer of designed antimicrobial peptide VG16KRKP

Analyse Disulphide linked homodimer of designed antimicrobial peptide VG16KRKP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2N65
Type
protein
Length
32 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Antimicrobial peptide VG16KRKP

Structure

solution nmr · 1 distinct chain · 0% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAntimicrobial peptide VG16KRKPprotein160% helix, 6% strand—

Interfaces

1 interface between chains.

  • A–B · 383 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 2N65 · Disulphide linked homodimer of designed antimicrobial peptide VG16KRKP · the same entry in another collection · chain A against A, TM-score 1.00

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