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The structure of human kinesin-like motor protein KIF11/KSP/EG5 in complex with ADP and enastrol.
Analyse The structure of human kinesin-like motor protein KIF11/KSP/EG5 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K5E
- Type
- protein
- Length
- 653 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinesin-like protein KIF11
- EC
- 3.6.4.4
- UniProt
- P52732
- Ligands
- K5E, ADP, MG
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinesin-like protein KIF11 (EC 3.6.4.4) | protein | 329 | 33% helix, 29% strand | P52732 |
| B | Kinesin-like protein KIF11 (EC 3.6.4.4) | protein | 324 | 34% helix, 30% strand | P52732 |
Ligands and binding sites
- K5E · (4S,5R)-5-hydroxy-4-(3-hydroxyphenyl)-3,4,5,6,7,8-hexahydroquinazoline-2(1H)-thione · ligand · 2 copies · chains A, B
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 955 | 0.81 | 0.82 | 116 | K5E, ADP, MG |
| 2 | 341 | 0.62 | 0.78 | 35 | empty |
| 3 | 321 | 0.59 | 0.77 | 31 | empty |
| 4 | 153 | 0.42 | 0.74 | 28 | empty |
| 5 | 121 | 0.38 | 0.74 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 963 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 3K5E · The structure of human kinesin-like motor protein Kif11/KSP/Eg5 in complex with ADP and… · 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 P52732
- Elsewhere: RCSB PDB 3K5E · PDBe 3K5E · UniProt P52732
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