MolNFT v1 · #60314 · protein
Structural dynamics of the microtubule binding and regulatory elements in the kinesin-like calmodulin binding protein
3CNZ · Kinesin heavy chain-like protein: “Structural dynamics of the microtubule binding and regulatory elements in the kinesin-like calmodulin binding…”. X-ray diffraction, 2 ligands (ADP, MG), 9 pockets (best druggability 0.59). MolNFT…
- PDB
- 3CNZ
- Type
- protein
- Length
- 664 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
- 9 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinesin heavy chain-like protein | protein | 333 | 29% helix, 26% strand | Q41460 |
| B | Kinesin heavy chain-like protein | protein | 331 | 30% helix, 23% strand | Q41460 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 335 | 0.59 | 0.77 | 48 | ADP, MG |
| 2 | 274 | 0.52 | 0.75 | 31 | empty |
| 3 | 175 | 0.51 | 0.78 | 31 | ADP, MG |
| 4 | 177 | 0.47 | 0.76 | 25 | empty |
| 5 | 64 | 0.46 | 0.83 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 492 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3CNZ · 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 3CNZ · PDBe 3CNZ · UniProt Q41460
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