Research workbench
Crystal structure of the 4-helix coiled coil cc-tet
Analyse Crystal structure of the 4-helix coiled coil cc-tet in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3R4A
- Type
- protein
- Length
- 117 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coiled coil helix cc-tet
Structure
x-ray diffraction · 3 distinct chains · 90% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coiled coil helix cc-tet | protein | 28 | 86% helix, 0% strand | — |
| B, C | Coiled coil helix cc-tet | protein | 30 | 93% helix, 0% strand | — |
| D | Coiled coil helix cc-tet | protein | 29 | 90% helix, 0% strand | — |
Interfaces
5 interfaces between chains.
- B–C · 743 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 726 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 542 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 516 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 231 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3R4A · Crystal structure of the 4-helix coiled coil CC-tet · 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 3R4A · PDBe 3R4A
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.