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Human death-associated kinase drp-1, mutant S308D D40

Analyse Human death-associated kinase drp-1, mutant S308D D40 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WMK
Type: protein
Length: 2,467 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Death-associated protein kinase 2
EC: 2.7.1.37
UniProt: Q9UIK4
Pockets: 20 · best druggability 0.79

Structure

x-ray diffraction · 4 distinct chains · 35% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, F	Death-associated protein kinase 2 (EC 2.7.1.37)	protein	303	34% helix, 16% strand	Q9UIK4
E, G	Death-associated protein kinase 2 (EC 2.7.1.37)	protein	313	35% helix, 16% strand	Q9UIK4
B, D	Death-associated protein kinase 2 (EC 2.7.1.37)	protein	314	34% helix, 15% strand	Q9UIK4
H	Death-associated protein kinase 2 (EC 2.7.1.37)	protein	304	35% helix, 17% strand	Q9UIK4

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	847	0.79	0.81	76	empty
2	767	0.78	0.82	63	empty
3	794	0.77	0.81	64	empty
4	780	0.77	0.81	65	empty
5	864	0.77	0.80	67	empty

Interfaces

10 interfaces between chains.

H–G · 1725 Å² buried · 11 hydrogen bonds · protein-protein
A–E · 1693 Å² buried · 10 hydrogen bonds · protein-protein
F–D · 1639 Å² buried · 7 hydrogen bonds · protein-protein
C–B · 1637 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 402 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

1WMK · Human death-associated kinase DRP-1, mutant S308D d40 · the same entry in another collection · chain G against G, TM-score 1.00
Q9UIK4 · AlphaFold monomer V2.0 prediction for death-associated protein kinase 2 (Q9UIK4) · a predicted model of the same protein · chain C against A, TM-score 0.99

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 Q9UIK4
Elsewhere: RCSB PDB 1WMK · PDBe 1WMK · UniProt Q9UIK4

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