MolNFT v1 · #13007 · protein
Crystal structure of a de novo designed trimeric coiled-coil peptide stablized by ionic interactions
1KYC · Sin-glu-glu-leu-arg-arg-arg-ile-glu-glu-leu-glu-arg-arg…: “Crystal structure of a de novo designed trimeric coiled-coil peptide stablized by ionic interactions”. X-ray diffraction, 2 ligands (SO4, NH2). MolNFT v1 #13007 on…
- PDB
- 1KYC
- Type
- protein
- Length
- 15 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sin-glu-glu-leu-arg-arg-arg-ile-glu-glu-leu-glu-arg-arg- ile-arg-NH2
- Ligands
- SO4, NH2
Structure
x-ray diffraction · 1 distinct chain · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sin-glu-glu-leu-arg-arg-arg-ile-glu-glu-leu-glu-arg-arg- ile-arg-NH2 | protein | 15 | 87% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
- NH2 · Amino group · ion · chains A
- SIN · Succinic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 1KYC · Crystal structure of a de novo designed trimeric coiled-coil peptide stablized by ionic… · 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 1KYC · PDBe 1KYC
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