Research workbench
Plk-1 polo-box domain in complex with histidine N(tau)-cyclized Macrocycle 5b.
Analyse Plk-1 polo-box domain in complex with histidine N(tau)-cyclized Macrocycle 5b. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AX4
- Type
- protein
- Length
- 226 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.45
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- Molecule
- Serine/threonine-protein kinase PLK1; histidine N(tau)-cyclized Macrocycle 5b
- EC
- 2.7.11.21
- UniProt
- P53350
- Ligands
- AML
Structure
x-ray diffraction · resolution 1.45 · 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 | 221 | 30% helix, 29% strand | P53350 |
| C | histidine N(tau)-cyclized Macrocycle 5b | protein | 5 | 0% helix, 20% strand | — |
Ligands and binding sites
- AML · Amylamine · ligand · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–C · 648 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified, 2 covalent (covalent ligand, nonstandard, phosphorylation).
Compared structures
- 6AX4 · Plk-1 polo-box domain in complex with histidine N(TAU)-cyclized macrocycle 5B. · the same entry in another collection · chain A against A, TM-score 1.00
- P53350 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase PLK1 (P53350) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 6AX4 · PDBe 6AX4 · UniProt P53350
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