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The solution structure of the nisin-lipid II complex

Analyse The solution structure of the nisin-lipid II complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WCO
Type: protein
Length: 39 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ala-fga-lys-dal-dal peptide; Lantibiotic
UniProt: Q7BB86
Ligands: MUB, FDF, NAG

Structure

solution nmr · 2 distinct chains · 10% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	Ala-fga-lys-dal-dal peptide	protein	5	0% helix, 0% strand	—
N	Lantibiotic	protein	34	12% helix, 0% strand	Q7BB86

Ligands and binding sites

MUB · N-acetyl-alpha-muramic acid · ligand · chains L, N
FDF · (2E,6E)-12-fluoro-11-(fluoromethyl)-3,7-dimethyldodeca-2,6,10-trien-1-yl trihydrogen diphosphate · ligand · chains L, N
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains L

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

Interfaces

1 interface between chains.

L–N · 193 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 8 modified, 3 d-amino, 1 covalent (nonstandard, D-amino acid, covalent ligand).

Compared structures

1WCO · The solution structure of the nisin-lipid II complex · the same entry in another collection · chain L against L, TM-score 1.00

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 Q7BB86
Elsewhere: RCSB PDB 1WCO · PDBe 1WCO · UniProt Q7BB86

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