Research workbench
Asymmetric antiparallel assembly of two 5-bladed beta-propeller fragments
Analyse Asymmetric antiparallel assembly of two 5-bladed beta-propeller fragments in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R60
- Type
- protein
- Length
- 748 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wd-40 repeat protein
- UniProt
- B2J0I0
- Pockets
- 6 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 3% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Wd-40 repeat protein | protein | 199 | 0% helix, 55% strand | B2J0I0 |
| B | Wd-40 repeat protein | protein | 176 | 4% helix, 51% strand | B2J0I0 |
| D | Wd-40 repeat protein | protein | 174 | 4% helix, 51% strand | B2J0I0 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1078 | 0.80 | 0.82 | 73 | empty |
| 2 | 1093 | 0.80 | 0.81 | 73 | empty |
| 3 | 388 | 0.65 | 0.79 | 45 | empty |
| 4 | 200 | 0.59 | 0.81 | 24 | empty |
| 5 | 119 | 0.40 | 0.75 | 22 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1432 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 1326 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 265 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 255 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 84 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6R60 · asymmetric antiparallel assembly of two 5-bladed beta-propeller fragments · 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 B2J0I0
- Elsewhere: RCSB PDB 6R60 · PDBe 6R60 · UniProt B2J0I0
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