MolNFT v1 · #14781 · protein
Human kinesin motor domain with docked neck linker
1MKJ · Kinesin heavy chain: “Human kinesin motor domain with docked neck linker”. X-ray diffraction, 3 ligands (ADP, MG, SO4), 3 pockets (best druggability 0.58). MolNFT v1 #14781 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1MKJ
- Type
- protein
- Length
- 336 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinesin heavy chain
- UniProt
- P33176
- Ligands
- ADP, MG, SO4
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinesin heavy chain | protein | 336 | 35% helix, 30% strand | P33176 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 188 | 0.58 | 0.81 | 34 | empty |
| 2 | 123 | 0.42 | 0.77 | 29 | MG, SO4, ADP |
| 3 | 70 | 0.33 | 0.75 | 14 | empty |
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 P33176
- Elsewhere: RCSB PDB 1MKJ · PDBe 1MKJ · UniProt P33176
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