Research workbench
Crystal structure of an antiparallel octameric transmembrane coiled coil K2-cctm-vbic
Analyse Crystal structure of an antiparallel octameric transmembrane coiled coil… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YB1
- Type
- protein
- Length
- 124 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- K2-cctm-vbic
- Ligands
- ACE, GLY, NH2
Structure
x-ray diffraction · 1 distinct chain · 94% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | K2-cctm-vbic | protein | 31 | 94% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 4 copies · chains A, B, C, D
- GLY · Glycine · ligand · 2 copies · chains B, C
- NH2 · Amino group · ion · 4 copies · chains A, B, C, D
- 2PE · Nonaethylene glycol · additive · 2 copies · chains B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- C–D · 687 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 686 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 605 Ų buried · 29 hydrogen bonds · protein-protein
- A–D · 583 Ų buried · 34 hydrogen bonds · protein-protein
- A–C · 86 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent (covalent ligand).
Compared structures
- 6YB1 · Crystal structure of an antiparallel octameric transmembrane coiled coil K2-CCTM-VbIc · the same entry in another collection · chain B against B, 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 6YB1 · PDBe 6YB1
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