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Structure of the fungal plasma membrane proton pump PMA1 in its auto- inhibited state - monomer unit

Analyse Structure of the fungal plasma membrane proton pump PMA1 in its auto- inhibited… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NXF
Type: protein
Length: 829 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Plasma membrane ATPase
EC: 7.1.2.1
UniProt: A0A0B0DXJ0
Ligands: ADP, MG, K
Pockets: 10 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 46% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Plasma membrane ATPase (EC 7.1.2.1)	protein	829	46% helix, 12% strand	A0A0B0DXJ0

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
K · Potassium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

10 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	1118	0.78	0.80	92	ADP, MG
2	210	0.61	0.81	37	empty
3	371	0.59	0.76	33	empty
4	321	0.56	0.76	51	empty
5	127	0.53	0.81	18	empty

Compared structures

7NXF · Structure of the fungal plasma membrane proton pump Pma1 in its auto-inhibited state… · 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 A0A0B0DXJ0
Elsewhere: RCSB PDB 7NXF · PDBe 7NXF · UniProt A0A0B0DXJ0

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