Research workbench
Crystal structure of the kinesin-14 NCDG347D
Analyse Crystal structure of the kinesin-14 NCDG347D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3U06
- Type
- protein
- Length
- 703 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein claret segregational
- UniProt
- P20480
- Ligands
- ADP, MG
- Pockets
- 11 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein claret segregational | protein | 359 | 44% helix, 26% strand | P20480 |
| B | Protein claret segregational | protein | 344 | 45% helix, 24% strand | P20480 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · chains A
- GOL · Glycerol · additive · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.59 | 0.84 | 27 | empty |
| 2 | 154 | 0.58 | 0.82 | 24 | empty |
| 3 | 157 | 0.55 | 0.81 | 31 | empty |
| 4 | 82 | 0.44 | 0.80 | 20 | empty |
| 5 | 132 | 0.44 | 0.76 | 16 | GOL |
Interfaces
1 interface between chains.
- A–B · 1731 Ų buried · 14 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 P20480
- Elsewhere: RCSB PDB 3U06 · PDBe 3U06 · UniProt P20480
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