Research workbench
Arginine containing reengineered coiled-coiled dimer to examine the impact of proximal cation identity on hydrophobically-driven assembly
Analyse Arginine containing reengineered coiled-coiled dimer to examine the impact of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OWD
- Type
- protein
- Length
- 56 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Ligands
- ACE, CL, NH2
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 28 | — | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 5 copies · chains A, B
- NH2 · Amino group · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6OWD · Arginine Containing Reengineered Coiled-Coiled Dimer to Examine the Impact of Proximal… · 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 6OWD · PDBe 6OWD
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