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18 NMR structures of ACAMP2-like peptide with non natural fluoroaromatic residue (ACAMP2F18PFF/Y20PFF) complex with N,N,N- triacetylchitotriose
Analyse 18 NMR structures of ACAMP2-like peptide with non natural fluoroaromatic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZNT
- Type
- protein
- Length
- 30 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amaranthus caudatus antimicrobial peptide 2
- Ligands
- NAG, NH2
Structure
solution nmr · 1 distinct chain · 13% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amaranthus caudatus antimicrobial peptide 2 | protein | 30 | 13% helix, 20% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · 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: 3 disulfide, 2 modified (disulfide, nonstandard).
Compared structures
- 1ZNT · 18 NMR structures of AcAMP2-Like Peptide with non Natural Fluoroaromatic Residue… · the same entry in another collection · chain A against A, 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
- Elsewhere: RCSB PDB 1ZNT · PDBe 1ZNT
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