Research workbench
KIF14[391-743] - ADP in complex with a microtubule
Analyse KIF14[391-743] - ADP in complex with a microtubule in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WWQ
- Type
- protein
- Length
- 1,215 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin alpha-1B chain; Tubulin beta-2B chain; Kinesin-like protein KIF14
- UniProt
- Q2XVP4, A0A287AGU7, L0N7N1
- Ligands
- GTP, GDP, TA1, ADP, MG
- Pockets
- 15 · best druggability 0.84
Structure
electron microscopy · 3 distinct chains · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin alpha-1B chain | protein | 441 | 42% helix, 13% strand | Q2XVP4 |
| B | Tubulin beta-2B chain | protein | 428 | 47% helix, 14% strand | A0A287AGU7 |
| K | Kinesin-like protein KIF14 | protein | 346 | 29% helix, 24% strand | L0N7N1 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · chains A, B
- GDP · Guanosine-5'-diphosphate · ligand · chains B
- TA1 · Taxol · ligand · chains B
- ADP · Adenosine-5'-diphosphate · ligand · chains K
- MG · Magnesium ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 271 | 0.84 | 0.95 | 43 | GTP, MG |
| 2 | 1092 | 0.80 | 0.81 | 74 | empty |
| 3 | 478 | 0.70 | 0.81 | 55 | empty |
| 4 | 273 | 0.61 | 0.80 | 36 | GDP |
| 5 | 179 | 0.60 | 0.82 | 25 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1983 Ų buried · 23 hydrogen bonds · protein-protein
- A–K · 1011 Ų buried · 7 hydrogen bonds · protein-protein
- B–K · 645 Ų buried · 7 hydrogen bonds · 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 Q2XVP4
- Every structure of UniProt A0A287AGU7
- Every structure of UniProt L0N7N1
- Elsewhere: RCSB PDB 6WWQ · PDBe 6WWQ · UniProt Q2XVP4 · UniProt A0A287AGU7 · UniProt L0N7N1
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