Research workbench
A de novo pentameric coiled-coil assembly: cc-TYPE2-(TGLAID)4- W19BRPHE.
Analyse A de novo pentameric coiled-coil assembly: cc-TYPE2-(TGLAID)4- W19BRPHE. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BAS
- Type
- protein
- Length
- 148 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cc-TYPE2-(TGLAID)4-W19BRPHE.
- Ligands
- ACE, NH2
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 92% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E | Cc-TYPE2-(TGLAID)4-W19BRPHE. | protein | 30 | 90% helix, 0% strand | — |
| C, D | Cc-TYPE2-(TGLAID)4-W19BRPHE. | protein | 29 | 93% helix, 0% strand | — |
Ligands and binding sites
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 | 50 | 0.66 | 0.94 | 15 | empty |
| 2 | 68 | 0.63 | 0.90 | 20 | empty |
Interfaces
10 interfaces between chains.
- B–E · 745 Ų buried · 3 hydrogen bonds · protein-protein
- A–E · 725 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 689 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 688 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 645 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified, 1 covalent (nonstandard, covalent ligand).
Compared structures
- 7BAS · A de novo pentameric coiled-coil assembly: CC-Type2-(TgLaId)4-W19BrPhe. · 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 7BAS · PDBe 7BAS
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