MolNFT v1 · #61095 · protein

Crystal structure of an activated (thr->asp) polo-like kinase 1 (PLK1) catalytic domain in complex with compound 557

3DBE: “Crystal structure of an activated (thr->asp) polo-like kinase 1 (PLK1) catalytic domain in complex with…”. X-ray diffraction, 1 ligand (4FR), 2 pockets (best druggability 0.70). MolNFT v1 #61095 on GenesisL1: 3D structure, binding…

PDB: 3DBE
Type: protein
Length: 284 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
Ligands: 4FR
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polo-like kinase 1 (EC 2.7.11.21)	protein	284	36% helix, 20% strand	Q4KMI8

Ligands and binding sites

4FR · 3'-chloro-5'-[6-({2-methoxy-4-[(1-methylpiperidin-4-yl)carbamoyl]phenyl}amino)-3-methyl-1H-pyrazolo[4,3-c]pyridin-1-yl]biphenyl-2-carboxamide · ligand · chains A

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	461	0.70	0.80	46	4FR
2	120	0.45	0.77	22	empty

Compared structures

3DBE · Crystal structure of an activated (Thr->Asp) 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 3DBE · PDBe 3DBE · UniProt Q4KMI8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.