Research workbench
Crystal structure of a wildtype polo-like kinase 1 (PLK1) catalytic domain.
Analyse Crystal structure of a wildtype polo-like kinase 1 (PLK1) catalytic domain. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D5U
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polo-like kinase 1
- EC
- 2.7.11.21
- UniProt
- Q4KMI8
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polo-like kinase 1 (EC 2.7.11.21) | protein | 288 | 36% helix, 18% strand | Q4KMI8 |
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 | 461 | 0.70 | 0.80 | 47 | empty |
| 2 | 79 | 0.42 | 0.80 | 17 | empty |
| 3 | 81 | 0.36 | 0.76 | 19 | empty |
Compared structures
- 3D5U · Crystal structure of a wildtype Polo-like kinase 1 (Plk1) catalytic domain. · 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 Q4KMI8
- Elsewhere: RCSB PDB 3D5U · PDBe 3D5U · UniProt Q4KMI8
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