Research workbench
Crystal structure of human kinesin EG5 in complex with (R)-fluorastrol
Analyse Crystal structure of human kinesin EG5 in complex with (R)-fluorastrol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X7E
- Type
- protein
- Length
- 668 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinesin-like protein KIF11
- UniProt
- P52732
- Ligands
- ADP, X7E, MG
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinesin-like protein KIF11 | protein | 333 | 33% helix, 32% strand | P52732 |
| B | Kinesin-like protein KIF11 | protein | 335 | 33% helix, 29% strand | P52732 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- X7E · (4R)-5-[(S)-(3,4-difluorophenyl)(hydroxy)methyl]-4-(3-hydroxyphenyl)-1,6-dimethyl-3,4-dihydropyrimidine-2(1H)-thione · 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 958 | 0.70 | 0.75 | 77 | empty |
| 2 | 290 | 0.62 | 0.80 | 51 | ADP, MG, X7E |
| 3 | 386 | 0.62 | 0.77 | 35 | empty |
| 4 | 222 | 0.60 | 0.81 | 39 | MG, X7E |
| 5 | 286 | 0.56 | 0.77 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 248 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2X7E · Crystal structure of human kinesin Eg5 in complex with (R)-fluorastrol · 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 2X7E · PDBe 2X7E · UniProt P52732
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