MolNFT v1 · #94482 · protein
Crystal structure of PLK1 polo-box domain in complex with pl-42
4HY2 · SERINE/THREONINE-protein kinase PLK1: “Crystal structure of PLK1 polo-box domain in complex with pl-42”. X-ray diffraction, 1 ligand (NH2). MolNFT v1 #94482 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4HY2
- Type
- protein
- Length
- 221 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase PLK1; Pl-42
- EC
- 2.7.11.21
- UniProt
- P53350
- Ligands
- NH2
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase PLK1 (EC 2.7.11.21) | protein | 215 | 30% helix, 30% strand | P53350 |
| D | Pl-42 | protein | 6 | 0% helix, 17% strand | — |
Ligands and binding sites
- NH2 · Amino group · ion · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–D · 518 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard, phosphorylation).
Compared structures
- 4HY2 · Crystal structure of Plk1 Polo-box domain in complex with PL-42 · 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 4HY2 · PDBe 4HY2 · UniProt P53350
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