Research workbench
HYL-20
Analyse HYL-20 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MMK
- Type
- protein
- Length
- 16 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gly-ile-leu-ser-ser-leu-TRP-lys-lys-leu-lys-lys-ile-ile- ala-lys
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gly-ile-leu-ser-ser-leu-TRP-lys-lys-leu-lys-lys-ile-ile- ala-lys | protein | 16 | 81% helix, 0% 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
- 5MMK · HYL-20 · 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 5MMK · PDBe 5MMK
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