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Polo-like kinase 1 polo box domain in complex with a C6H5(CH2)8- derivatized peptide inhibitor

Analyse Polo-like kinase 1 polo box domain in complex with a C6H5(CH2)8- derivatized… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3RQ7
Type: protein
Length: 217 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase PLK1; C6H5(CH2)8-derivatized peptide inhibitor
EC: 2.7.11.21
UniProt: P53350
Ligands: ACE, NH2

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase PLK1 (EC 2.7.11.21)	protein	212	31% helix, 31% strand	P53350
B	C6H5(CH2)8-derivatized peptide inhibitor	protein	5	0% helix, 20% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · chains A, B
NH2 · Amino group · ion · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 642 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified, 1 covalent (covalent ligand, nonstandard, phosphorylation).

Compared structures

3RQ7 · Polo-like kinase 1 Polo box domain in complex with a C6H5(CH2)8-derivatized peptide… · 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 3RQ7 · PDBe 3RQ7 · UniProt P53350

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