Research workbench

Crystal structure of DAPK1 in complex with 7,3',4'- trihydroxyisoflavone.

Analyse Crystal structure of DAPK1 in complex with 7,3',4'- trihydroxyisoflavone. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5AV0
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Death-associated protein kinase 1
EC: 2.7.11.1
UniProt: P53355
Ligands: 47X
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Death-associated protein kinase 1 (EC 2.7.11.1)	protein	275	36% helix, 20% strand	P53355

Ligands and binding sites

47X · 3-(3,4-dihydroxyphenyl)-7-hydroxy-4H-chromen-4-one · 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	415	0.69	0.81	47	47X
2	65	0.29	0.73	15	empty

Compared structures

5AV0 · Crystal structure of DAPK1 in complex with 7,3',4'-trihydroxyisoflavone. · the same entry in another collection · chain A against A, TM-score 1.00
P53355 · AlphaFold monomer V2.0 prediction for death-associated protein kinase 1 (P53355) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P53355
Elsewhere: RCSB PDB 5AV0 · PDBe 5AV0 · UniProt P53355

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.