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The NMR-derived conformation of neuropeptide F from moniezia expansa

Analyse The NMR-derived conformation of neuropeptide F from moniezia expansa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1K8V
Type: protein
Length: 39 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neuropeptide F
UniProt: P41967
Ligands: NH2

Structure

solution nmr · 1 distinct chain · 44% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Neuropeptide F	protein	39	44% helix, 0% strand	P41967

Ligands and binding sites

NH2 · Amino group · ion · chains A

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

Compared structures

1K8V · The NMR-derived Conformation of Neuropeptide F from Moniezia expansa · the same entry in another collection · chain A against A, TM-score 1.00
P41967 · AlphaFold monomer V2.0 prediction for neuropeptide F (P41967) · a predicted model of the same protein · chain A against A, TM-score 0.37

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P41967
Elsewhere: RCSB PDB 1K8V · PDBe 1K8V · UniProt P41967

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