Research workbench
Porous framework formed by assembly of a bipyridyl-conjugated helical peptide
Analyse Porous framework formed by assembly of a bipyridyl-conjugated helical peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TMK
- Type
- protein
- Length
- 18 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Helical peptide
- Ligands
- CCN, I77, I6W
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Helical peptide | protein | 9 | 56% helix, 0% strand | — |
Ligands and binding sites
- CCN · Acetonitrile · ligand · 3 copies · chains A, C
- I77 · 5'-(hydrazinecarbonyl)[2,2'-bipyridine]-5-carboxamide · ligand · 2 copies · chains A, C
- I6W · Ethyl 5'-formyl[2,2'-bipyridine]-5-carboxylate · ligand · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 6 modified, 4 covalent (nonstandard, covalent ligand).
Compared structures
- 7TMK · Porous framework formed by assembly of a bipyridyl-conjugated helical peptide · 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 7TMK · PDBe 7TMK
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