Research workbench
Structural dynamics of the microtubule binding and regulatory elements in the kinesin-like calmodulin binding protein
Analyse Structural dynamics of the microtubule binding and regulatory elements in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3COB
- Type
- protein
- Length
- 695 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinesin heavy chain-like protein
- UniProt
- Q41460
- Ligands
- ADP, MG
- Pockets
- 7 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinesin heavy chain-like protein | protein | 355 | 32% helix, 27% strand | Q41460 |
| C | Kinesin heavy chain-like protein | protein | 340 | 31% helix, 30% strand | Q41460 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, C
- MG · Magnesium ion · metal · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.57 | 0.77 | 45 | ADP, MG |
| 2 | 329 | 0.56 | 0.76 | 43 | ADP, MG |
| 3 | 269 | 0.55 | 0.76 | 29 | empty |
| 4 | 263 | 0.50 | 0.74 | 35 | empty |
| 5 | 66 | 0.38 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–C · 345 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3COB · Structural Dynamics of the Microtubule binding and regulatory elements in the… · 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 Q41460
- Elsewhere: RCSB PDB 3COB · PDBe 3COB · UniProt Q41460
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