MolNFT v1 · #127889 · protein

Ttk kinase domain in complex with a peg-linked pyrimido-indolizine

5NA0 · Dual specificity protein kinase ttk: “Ttk kinase domain in complex with a peg-linked pyrimido-indolizine”. X-ray diffraction, 1 ligand (8QZ), 1 pocket (best druggability 0.69). MolNFT v1 #127889 on GenesisL1: 3D structure, binding…

PDB: 5NA0
Type: protein
Length: 254 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dual specificity protein kinase ttk
EC: 2.7.12.1
UniProt: P33981
Ligands: 8QZ
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dual specificity protein kinase ttk (EC 2.7.12.1)	protein	254	37% helix, 21% strand	P33981

Ligands and binding sites

8QZ · ~{N}-[3,5-diethyl-1-[2-[2-(2-methoxyethoxy) ethoxy]ethyl]pyrazol-4-yl]-2-[[2-methoxy-4-[4-(2-methoxyethanoyl)piperazin-1-yl]phenyl]amino]-5,6-dihydropyrimido[4,5-e]indolizine-7-carboxamide · 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	485	0.69	0.80	42	8QZ

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

5NA0 · TTK kinase domain in complex with a PEG-linked pyrimido-indolizine · 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 P33981
Elsewhere: RCSB PDB 5NA0 · PDBe 5NA0 · UniProt P33981

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