MolNFT v1 · #128079 · protein
The structure of the polo-box domain (pbd) of polo-like kinase 1 (PLK1) in complex with lhspta peptide.
5NFU · SERINE/THREONINE-protein kinase PLK1: “The structure of the polo-box domain (pbd) of polo-like kinase 1 (PLK1) in complex with lhspta peptide.”. X-ray diffraction, 1 pocket (best druggability 0.43). MolNFT v1 #128079 on GenesisL1…
- PDB
- 5NFU
- Type
- protein
- Length
- 228 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase PLK1; Ac-leu-his-ser-(tpo)-ala
- EC
- 2.7.11.21
- UniProt
- P53350
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase PLK1 (EC 2.7.11.21) | protein | 223 | 31% helix, 29% strand | P53350 |
| C | Ac-leu-his-ser-(tpo)-ala | protein | 5 | 0% helix, 0% strand | — |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.43 | 0.75 | 30 | empty |
Interfaces
1 interface between chains.
- A–C · 462 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard, phosphorylation).
Compared structures
- 5NFU · The structure of the polo-box domain (PBD) of polo-like kinase 1 (Plk1) in complex with… · 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 P53350
- Elsewhere: RCSB PDB 5NFU · PDBe 5NFU · UniProt P53350
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.