Research workbench
Crystal structure of an antiparallel five-helix coiled coil 5H2L_2.1- I9L
Analyse Crystal structure of an antiparallel five-helix coiled coil 5H2L_2.1- I9L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G6H
- Type
- protein
- Length
- 165 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5H2L_2.1-I9L
- Ligands
- ACE, NH2
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 94% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | 5H2L_2.1-I9L | protein | 33 | 94% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 5 copies · chains A, B, C, D, E
- NH2 · Amino group · ion · 4 copies · chains A, E, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.72 | 0.91 | 29 | empty |
| 2 | 162 | 0.69 | 0.87 | 20 | empty |
Interfaces
10 interfaces between chains.
- A–E · 976 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 944 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 916 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 902 Ų buried · 1 hydrogen bond · protein-protein
- D–E · 897 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 covalent (covalent ligand).
Compared structures
- 6G6H · Crystal structure of an antiparallel five-helix coiled coil 5H2L_2.1-I9L · 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 6G6H · PDBe 6G6H
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