Research workbench

Cryo-EM structure of ATP13A2 D458N/D962N mutant in the E1-apo state, conformation 2

Analyse Cryo-EM structure of ATP13A2 D458N/D962N mutant in the E1-apo state… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7N76
Type: protein
Length: 1,036 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isoform 3 of polyamine-transporting ATPase 13A2
EC: 7.6.2.-
UniProt: Q9NQ11
Pockets: 15 · best druggability 0.73

Structure

electron microscopy · 1 distinct chain · 46% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Isoform 3 of polyamine-transporting ATPase 13A2 (EC 7.6.2.-)	protein	1036	46% helix, 19% strand	Q9NQ11

Pockets

15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	595	0.73	0.81	94	empty
2	805	0.71	0.77	84	empty
3	179	0.64	0.85	32	empty
4	405	0.62	0.77	48	empty
5	114	0.61	0.87	22	empty

Compared structures

7N76 · Cryo-EM structure of ATP13A2 D458N/D962N mutant in the E1-apo state, Conformation 2 · the same entry in another collection · chain A against A, TM-score 1.00
Q9NQ11 · AlphaFold monomer V2.0 prediction for polyamine-transporting ATPase 13A2 (Q9NQ11) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q9NQ11
Elsewhere: RCSB PDB 7N76 · PDBe 7N76 · UniProt Q9NQ11

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