MolNFT v1 · #129831 · protein
P60P80-camsap complex
5OW5 · Katanin P80 WD40 repeat-containing subunit B1: “P60P80-camsap complex”. X-ray diffraction, 6 pockets (best druggability 0.52). MolNFT v1 #129831 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OW5
- Type
- protein
- Length
- 504 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Katanin P80 WD40 repeat-containing subunit B1; Katanin P60 ATPase-containing subunit A1…
- EC
- 3.6.4.3
- UniProt
- Q8BG40, E9PZI6
- Pockets
- 6 · best druggability 0.52
Structure
x-ray diffraction · 5 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Katanin P80 WD40 repeat-containing subunit B1 | protein | 170 | 78% helix, 0% strand | Q8BG40 |
| B | Katanin P60 ATPase-containing subunit A1 (EC 3.6.4.3) | protein | 77 | 83% helix, 0% strand | E9PZI6 |
| C | Katanin P80 WD40 repeat-containing subunit B1 | protein | 165 | 80% helix, 0% strand | Q8BG40 |
| D | Katanin P60 ATPase-containing subunit A1 (EC 3.6.4.3) | protein | 72 | 88% helix, 0% strand | E9PZI6 |
| E, F | Calmodulin-regulated spectrin-associated protein | protein | 10 | 80% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.52 | 0.74 | 37 | PEG |
| 2 | 240 | 0.47 | 0.73 | 29 | empty |
| 3 | 79 | 0.34 | 0.75 | 16 | empty |
| 4 | 75 | 0.33 | 0.75 | 15 | empty |
| 5 | 75 | 0.31 | 0.73 | 14 | empty |
Interfaces
8 interfaces between chains.
- A–B · 1577 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 1484 Ų buried · 23 hydrogen bonds · protein-protein
- A–D · 430 Ų buried · 5 hydrogen bonds · protein-protein
- A–E · 347 Ų buried · 4 hydrogen bonds · protein-protein
- C–F · 325 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 Q8BG40
- Every structure of UniProt E9PZI6
- Elsewhere: RCSB PDB 5OW5 · PDBe 5OW5 · UniProt Q8BG40 · UniProt E9PZI6
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