Research workbench
Nucleotide-free kinesin-1 motor domain T92V mutant, P21 crystal form
Analyse Nucleotide-free kinesin-1 motor domain T92V mutant, P21 crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LT1
- Type
- protein
- Length
- 622 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinesin-like protein
- UniProt
- Q6P164
- Ligands
- SR, SO4
- Pockets
- 7 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinesin-like protein | protein | 309 | 34% helix, 28% strand | Q6P164 |
| B | Kinesin-like protein | protein | 313 | 35% helix, 28% strand | Q6P164 |
Ligands and binding sites
- SR · Strontium ion · metal · chains B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- ACT · Acetate ion · additive · 4 copies · chains A, B
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 | 624 | 0.69 | 0.78 | 53 | empty |
| 2 | 153 | 0.45 | 0.76 | 34 | empty |
| 3 | 74 | 0.42 | 0.80 | 20 | empty |
| 4 | 118 | 0.41 | 0.76 | 24 | SO4 |
| 5 | 106 | 0.40 | 0.76 | 24 | SO4, ACT |
Interfaces
1 interface between chains.
- A–B · 851 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 5LT1 · nucleotide-free kinesin-1 motor domain T92V mutant, P21 crystal form · 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 Q6P164
- Elsewhere: RCSB PDB 5LT1 · PDBe 5LT1 · UniProt Q6P164
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