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Proton pyrophosphatase-E225S mutant

Analyse Proton pyrophosphatase-E225S mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AFY
Type: protein
Length: 1,480 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P21616
Ligands: 1PG, MG, K, PO4

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	—	protein	740	—	P21616

Ligands and binding sites

1PG · 2-(2-{2-[2-(2-methoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethanol · ligand · 6 copies · chains A, B
MG · Magnesium ion · metal · 10 copies · chains A, B
K · Potassium ion · metal · 2 copies · chains A, B
PO4 · Phosphate ion · ion · 4 copies · chains A, B

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

Compared structures

6AFY · Proton pyrophosphatase-E225S mutant · the same entry in another collection · chain A against A, TM-score 1.00
P21616 · AlphaFold monomer V2.0 prediction for pyrophosphate-energized vacuolar membrane proton… · a predicted model of the same protein · chain B 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 P21616
Elsewhere: RCSB PDB 6AFY · PDBe 6AFY · UniProt P21616

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