MolNFT v1 · #138217 · protein
Katanin hexamer in spiral conformation
5WC0 · Meiotic spindle formation protein mei-1: “Katanin hexamer in spiral conformation”. Electron microscopy, 1 ligand (ATP), 20 pockets (best druggability 0.87). MolNFT v1 #138217 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5WC0
- Type
- protein
- Length
- 1,660 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Meiotic spindle formation protein mei-1
- EC
- 3.6.4.3
- UniProt
- P34808
- Ligands
- ATP
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 2 distinct chains · 44% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Meiotic spindle formation protein mei-1 (EC 3.6.4.3) | protein | 275 | 44% helix, 5% strand | P34808 |
| B, C, D, E, F | Meiotic spindle formation protein mei-1 (EC 3.6.4.3) | protein | 277 | 44% helix, 6% strand | P34808 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 942 | 0.87 | 0.88 | 151 | ATP |
| 2 | 888 | 0.84 | 0.86 | 124 | empty |
| 3 | 546 | 0.80 | 0.86 | 78 | ATP |
| 4 | 346 | 0.79 | 0.89 | 62 | empty |
| 5 | 428 | 0.76 | 0.85 | 55 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1611 Ų buried · 17 hydrogen bonds · protein-protein
- D–E · 1581 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 1550 Ų buried · 14 hydrogen bonds · protein-protein
- E–F · 1540 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1468 Ų buried · 12 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 P34808
- Elsewhere: RCSB PDB 5WC0 · PDBe 5WC0 · UniProt P34808
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