MolNFT v1 · #13510 · protein
NMR structure of tryptophan zipper 1: a stable, monomeric beta-hairpin with a type II' turn
1LE0: “NMR structure of tryptophan zipper 1: a stable, monomeric beta-hairpin with a type II' turn”. Solution nmr, 1 ligand (NH2). MolNFT v1 #13510 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1LE0
- Type
- protein
- Length
- 12 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophan zipper 1
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 0% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophan zipper 1 | protein | 12 | 0% helix, 50% strand | — |
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
- 1LE0 · NMR structure of Tryptophan Zipper 1: a stable, monomeric beta-hairpin with a type II'… · 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 1LE0 · PDBe 1LE0
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