Research workbench
Crystal structure of the mouse KIF14 motor domain
Analyse Crystal structure of the mouse KIF14 motor domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OZQ
- Type
- protein
- Length
- 1,370 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimera of maltose-binding periplasmic protein and kinesin family member 14 protein
- UniProt
- T9HUW4, L0N7N1
- Ligands
- ADP
- Pockets
- 16 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chimera of maltose-binding periplasmic protein and kinesin family member 14 protein | protein | 683 | 41% helix, 22% strand | T9HUW4, L0N7N1 |
| B | Chimera of maltose-binding periplasmic protein and kinesin family member 14 protein | protein | 687 | 40% helix, 24% strand | T9HUW4, L0N7N1 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 571 | 0.68 | 0.77 | 57 | empty |
| 2 | 542 | 0.66 | 0.77 | 64 | empty |
| 3 | 330 | 0.66 | 0.80 | 41 | empty |
| 4 | 116 | 0.64 | 0.87 | 18 | empty |
| 5 | 441 | 0.63 | 0.77 | 42 | empty |
Interfaces
1 interface between chains.
- A–B · 236 Ų buried · 1 hydrogen bond · 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 T9HUW4
- Every structure of UniProt L0N7N1
- Elsewhere: RCSB PDB 4OZQ · PDBe 4OZQ · UniProt T9HUW4 · UniProt L0N7N1
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