Research workbench
KLP10A-amppnp in complex with a microtubule
Analyse KLP10A-amppnp in complex with a microtubule in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B0L
- Type
- protein
- Length
- 1,238 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin alpha-1B chain; Tubulin beta chain; Kinesin-like protein KLP10A
- UniProt
- Q2XVP4, F2Z5B2, Q960Z0
- Ligands
- GTP, GDP, TA1, ANP, MG
- Pockets
- 16 · best druggability 0.87
Structure
electron microscopy · 3 distinct chains · 37% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin alpha-1B chain | protein | 441 | 40% helix, 10% strand | Q2XVP4 |
| B | Tubulin beta chain | protein | 429 | 42% helix, 16% strand | F2Z5B2 |
| K | Kinesin-like protein KLP10A | protein | 368 | 26% helix, 19% strand | Q960Z0 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · chains A, B
- GDP · Guanosine-5'-diphosphate · ligand · chains B
- TA1 · Taxol · ligand · chains B
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains K
- MG · Magnesium ion · metal · 2 copies · chains A, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 675 | 0.87 | 0.91 | 76 | empty |
| 2 | 266 | 0.84 | 0.95 | 51 | GTP, MG |
| 3 | 225 | 0.83 | 0.95 | 47 | empty |
| 4 | 221 | 0.77 | 0.92 | 44 | empty |
| 5 | 207 | 0.76 | 0.91 | 50 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2032 Ų buried · 14 hydrogen bonds · protein-protein
- A–K · 1012 Ų buried · 8 hydrogen bonds · protein-protein
- B–K · 897 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 Q2XVP4
- Every structure of UniProt F2Z5B2
- Every structure of UniProt Q960Z0
- Elsewhere: RCSB PDB 6B0L · PDBe 6B0L · UniProt Q2XVP4 · UniProt F2Z5B2 · UniProt Q960Z0
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