Research workbench
Proadrenomedullin N-terminal 20 peptide
Analyse Proadrenomedullin N-terminal 20 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FLY
- Type
- protein
- Length
- 20 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proadrenomedullin N-20 terminal peptide
- UniProt
- P35318
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 85% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proadrenomedullin N-20 terminal peptide | protein | 20 | 85% helix, 0% strand | P35318 |
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
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 P35318
- Elsewhere: RCSB PDB 2FLY · PDBe 2FLY · UniProt P35318
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