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Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant)

Analyse Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XSA
Type: protein
Length: 153 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BIS(5'-nucleosyl)-tetraphosphatase
EC: 3.6.1.17
UniProt: P50583
Pockets: 1 · best druggability 0.53

Structure

solution nmr · 1 distinct chain · 25% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BIS(5'-nucleosyl)-tetraphosphatase (EC 3.6.1.17)	protein	153	25% helix, 29% strand	P50583

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	252	0.53	0.76	34	empty

Compared structures

1XSA · Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant) · the same entry in another collection · chain A against A, TM-score 1.00
P50583 · AlphaFold monomer V2.0 prediction for BIS(5'-nucleosyl)-tetraphosphatase [asymmetrical]… · a predicted model of the same protein · chain A against A, TM-score 0.86

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 P50583
Elsewhere: RCSB PDB 1XSA · PDBe 1XSA · UniProt P50583

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