MolNFT v1 · #170250 · protein
Human EG5 motor domain mutant R234C
6Y1I · Kinesin-like protein KIF11: “Human EG5 motor domain mutant R234C”. X-ray diffraction, 2 ligands (ADP, MG), 12 pockets (best druggability 0.83). MolNFT v1 #170250 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6Y1I
- Type
- protein
- Length
- 971 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinesin-like protein KIF11
- UniProt
- P52732
- Ligands
- ADP, MG
- Pockets
- 12 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Kinesin-like protein KIF11 | protein | 326 | 33% helix, 25% strand | P52732 |
| B | Kinesin-like protein KIF11 | protein | 319 | 34% helix, 26% strand | P52732 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains A, B, C
- MG · Magnesium ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1169 | 0.83 | 0.84 | 100 | empty |
| 2 | 388 | 0.69 | 0.82 | 39 | empty |
| 3 | 291 | 0.57 | 0.77 | 33 | empty |
| 4 | 51 | 0.39 | 0.81 | 16 | empty |
| 5 | 74 | 0.35 | 0.77 | 21 | ADP, MG |
Interfaces
3 interfaces between chains.
- A–B · 674 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 324 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 196 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6Y1I · Human Eg5 motor domain mutant R234C · 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 6Y1I · PDBe 6Y1I · UniProt P52732
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