MolNFT v1 · #8026 · protein
Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules
1GOJ · Kinesin heavy chain: “Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules”. X-ray diffraction, 2 ligands (ADP, MG), 7 pockets (best druggability 0.60). MolNFT v1 #8026 on GenesisL1: 3D…
- PDB
- 1GOJ
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinesin heavy chain
- EC
- 3.6.4.4
- UniProt
- P48467
- Ligands
- ADP, MG
- Pockets
- 7 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinesin heavy chain (EC 3.6.4.4) | protein | 354 | 31% helix, 25% strand | P48467 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 248 | 0.60 | 0.80 | 30 | empty |
| 2 | 132 | 0.47 | 0.78 | 29 | empty |
| 3 | 50 | 0.43 | 0.84 | 15 | empty |
| 4 | 73 | 0.41 | 0.80 | 19 | empty |
| 5 | 80 | 0.38 | 0.77 | 21 | empty |
Compared structures
- 1GOJ · Structure of a fast kinesin: Implications for ATPase mechanism and interactions with… · the same entry in another collection · chain A against A, TM-score 1.00
- P48467 · AlphaFold monomer V2.0 prediction for kinesin heavy chain (P48467) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P48467
- Elsewhere: RCSB PDB 1GOJ · PDBe 1GOJ · UniProt P48467
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