MolNFT v1 · #102693 · protein

Crystal structure of PRK1 catalytic domain in complex with lestaurtinib

4OTG · SERINE/THREONINE-protein kinase N1: “Crystal structure of PRK1 catalytic domain in complex with lestaurtinib”. X-ray diffraction, 1 ligand (2V9), 2 pockets (best druggability 0.61). MolNFT v1 #102693 on GenesisL1: 3D structure…

PDB: 4OTG
Type: protein
Length: 324 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase N1
EC: 2.7.11.13
UniProt: Q16512
Ligands: 2V9
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase N1 (EC 2.7.11.13)	protein	324	35% helix, 15% strand	Q16512

Ligands and binding sites

2V9 · Lestaurtinib · 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	219	0.61	0.81	25	2V9
2	105	0.42	0.77	18	empty

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

4OTG · Crystal Structure of PRK1 Catalytic Domain in Complex with Lestaurtinib · the same entry in another collection · chain A against A, TM-score 1.00
Q16512 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase N1 (Q16512) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q16512
Elsewhere: RCSB PDB 4OTG · PDBe 4OTG · UniProt Q16512

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