Research workbench
Structure of antimicrobial peptide, hp (2-20) and its analogues derived from helicobacter pylori, as determined by 1H NMR spectroscopy
Analyse Structure of antimicrobial peptide, hp (2-20) and its analogues derived from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P0G
- Type
- protein
- Length
- 19 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 19-mer peptide from 50S ribosomal protein L1
- UniProt
- Q9ZK21
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 58% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 19-mer peptide from 50S ribosomal protein L1 | protein | 19 | 58% helix, 0% strand | Q9ZK21 |
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
- 1P0G · Structure of Antimicrobial Peptide, HP (2-20) and its Analogues Derived from Helicobacter… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ZK21 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L1 (Q9ZK21) · a predicted model of the same protein · chain A against A, TM-score 0.35
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 Q9ZK21
- Elsewhere: RCSB PDB 1P0G · PDBe 1P0G · UniProt Q9ZK21
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