MolNFT v1 · #60908 · protein

Crystal structure of a phosphorylated polo-like kinase 1 (PLK1) catalytic domain in complex with ADP.

3D5W: “Crystal structure of a phosphorylated polo-like kinase 1 (PLK1) catalytic domain in complex with ADP.”. X-ray diffraction, 1 ligand (ADP), 1 pocket (best druggability 0.70). MolNFT v1 #60908 on GenesisL1: 3D structure, binding sites…

PDB: 3D5W
Type: protein
Length: 285 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: ADP
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polo-like kinase 1 (EC 2.7.11.21)	protein	285	34% helix, 19% strand	Q4KMI8

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	423	0.70	0.81	41	ADP

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

3D5W · Crystal structure of a phosphorylated Polo-like kinase 1 (Plk1) catalytic domain in… · 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 3D5W · PDBe 3D5W · UniProt Q4KMI8

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