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Structural studies of D-pro melittin, NMR, 20 structures

Analyse Structural studies of D-pro melittin, NMR, 20 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BH1
Type: protein
Length: 26 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Melittin
UniProt: P01501
Ligands: NH2

Structure

solution nmr · 1 distinct chain · 50% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Melittin	protein	26	50% helix, 0% strand	P01501

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

1BH1 · Structural studies of D-pro melittin, NMR, 20 structures · the same entry in another collection · chain A against A, TM-score 1.00
P01501 · AlphaFold monomer V2.0 prediction for melittin (P01501) · a predicted model of the same protein · chain A against A, TM-score 0.32

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 P01501
Elsewhere: RCSB PDB 1BH1 · PDBe 1BH1 · UniProt P01501

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