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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 v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
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 · 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 Å² 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 C against C, 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 6AX4 · PDBe 6AX4 · UniProt P53350

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