Research workbench
TPX2 residues 7-20 fused to aurora a residues 116-389 dephosphorylated, and coalated on C290
Analyse TPX2 residues 7-20 fused to aurora a residues 116-389 dephosphorylated, and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XKA
- Type
- protein
- Length
- 252 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TPX2 fragment - aurora a kinase domain fusion
- EC
- 2.7.11.1
- UniProt
- Q9ULW0, O14965
- Ligands
- COA
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TPX2 fragment - aurora a kinase domain fusion (EC 2.7.11.1) | protein | 252 | 42% helix, 20% strand | Q9ULW0, O14965 |
Ligands and binding sites
- COA · Coenzyme A · ligand
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 380 | 0.63 | 0.78 | 35 | empty |
| 2 | 68 | 0.44 | 0.81 | 12 | empty |
| 3 | 148 | 0.40 | 0.73 | 25 | empty |
Compared structures
- 6XKA · TPX2 residues 7-20 fused to Aurora A residues 116-389 dephosphorylated, and CoAlated on… · the same entry in another collection · chain A against A, TM-score 1.00
- O14965 · AlphaFold monomer V2.0 prediction for aurora kinase a (O14965) · a predicted model of the same protein · chain A against A, TM-score 0.93
- Q9ULW0 · AlphaFold monomer V2.0 prediction for targeting protein for XKLP2 (Q9ULW0) · a predicted model of the same protein · chain A against A, TM-score 0.15
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 Q9ULW0
- Every structure of UniProt O14965
- Elsewhere: RCSB PDB 6XKA · PDBe 6XKA · UniProt Q9ULW0 · UniProt O14965
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.