MolNFT v1 · #61093 · protein

Crystal structure of an activated (thr->asp) polo-like kinase 1 (PLK1) catalytic domain in complex with compound 257

3DBC: “Crystal structure of an activated (thr->asp) polo-like kinase 1 (PLK1) catalytic domain in complex with…”. X-ray diffraction, 1 ligand (2FR), 2 pockets (best druggability 0.67). MolNFT v1 #61093 on GenesisL1: 3D structure, binding…

PDB: 3DBC
Type: protein
Length: 261 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: 2FR
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polo-like kinase 1 (EC 2.7.11.21)	protein	261	38% helix, 21% strand	Q4KMI8

Ligands and binding sites

2FR · 3-[3-(3-methyl-6-{[(1S)-1-phenylethyl]amino}-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanamide · 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	421	0.67	0.79	44	2FR
2	226	0.47	0.74	25	empty

Compared structures

3DBC · 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 3DBC · PDBe 3DBC · UniProt Q4KMI8

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