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Tankyrase-2 in complex with compound 52

Analyse Tankyrase-2 in complex with compound 52 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZQQ
Type: protein
Length: 209 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tankyrase-2
EC: 2.4.2.30
UniProt: Q9H2K2
Ligands: 9H6, ZN, PO4
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tankyrase-2 (EC 2.4.2.30)	protein	162	29% helix, 25% strand	Q9H2K2
B	Tankyrase-2 (EC 2.4.2.30)	protein	47	6% helix, 45% strand	Q9H2K2

Ligands and binding sites

9H6 · 1-methyl-1'-(4-oxo-3,4,5,6,7,8-hexahydroquinazolin-2-yl)spiro[indole-3,4'-piperidin]-2(1H)-one · ligand · chains A, B
ZN · Zinc ion · metal · chains A
PO4 · Phosphate ion · ion · chains A
GOL · Glycerol · additive · chains A, B

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	229	0.65	0.83	38	9H6, PO4

Interfaces

1 interface between chains.

A–B · 3059 Å² buried · 66 hydrogen bonds · protein-protein

Compared structures

5ZQQ · Tankyrase-2 in complex with compound 52 · 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 Q9H2K2
Elsewhere: RCSB PDB 5ZQQ · PDBe 5ZQQ · UniProt Q9H2K2

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