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Tetragonal crystal form of a catalytic domain of death-associated protein kinase

Analyse Tetragonal crystal form of a catalytic domain of death-associated protein kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JKT
Type: protein
Length: 552 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Death-associated protein kinase
EC: 2.7.1.-
UniProt: P53355
Pockets: 7 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Death-associated protein kinase (EC 2.7.1.-)	protein	276	31% helix, 14% strand	P53355

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	799	0.76	0.80	72	empty
2	506	0.70	0.80	48	empty
3	81	0.69	0.94	19	empty
4	119	0.60	0.85	23	empty
5	62	0.59	0.90	17	empty

Interfaces

1 interface between chains.

A–B · 730 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1JKT · Tetragonal crystal form of a catalytic domain of death-associated protein kinase · 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 0.95

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 1JKT · PDBe 1JKT · UniProt P53355

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