Research workbench
Crystal structure of MC159 reveals molecular mechanism of disc assembly and vflip inhibition
Analyse Crystal structure of MC159 reveals molecular mechanism of disc assembly and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BBZ
- Type
- protein
- Length
- 760 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Viral CASP8 and fadd-like apoptosis regulator
- UniProt
- Q98325
- Pockets
- 11 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Viral CASP8 and fadd-like apoptosis regulator | protein | 190 | 54% helix, 0% strand | Q98325 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 375 | 0.84 | 0.92 | 55 | empty |
| 2 | 74 | 0.67 | 0.93 | 26 | empty |
| 3 | 71 | 0.66 | 0.92 | 20 | empty |
| 4 | 74 | 0.66 | 0.92 | 25 | empty |
| 5 | 136 | 0.42 | 0.75 | 14 | empty |
Interfaces
6 interfaces between chains.
- C–D · 722 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 684 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 625 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 557 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 557 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2BBZ · Crystal Structure of MC159 Reveals Molecular Mechanism of DISC Assembly and vFLIP… · 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
- Every structure of UniProt Q98325
- Elsewhere: RCSB PDB 2BBZ · PDBe 2BBZ · UniProt Q98325
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