GL1X · GenesisL1 explorer

Research workbench

Stability of cyclic beta-hairpins: asymmetric contibutions from side chains of hydrogen bonded cross-strand residue pair

Analyse Stability of cyclic beta-hairpins: asymmetric contibutions from side chains of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1N0D
Type
protein
Length
10 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
BHP_VWLH, disulfide cyclized beta-hairpin peptide
Ligands
ACE, NH2

Structure

solution nmr · 1 distinct chain · 0% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABHP_VWLH, disulfide cyclized beta-hairpin peptideprotein100% helix, 40% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A
  • NH2 · Amino group · ion · chains A

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

Modifications

Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).

Compared structures

  • 1N0D · Stability of cyclic beta-hairpins: Asymmetric contibutions from side chains of hydrogen… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.