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Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant) in complex with ATP

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

PDB: 1XSC
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
Ligands: ATP
Pockets: 2 · best druggability 0.38

Structure

solution nmr · 1 distinct chain · 24% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BIS(5'-nucleosyl)-tetraphosphatase (EC 3.6.1.17)	protein	153	24% helix, 27% strand	P50583

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.38	0.78	20	empty
2	85	0.32	0.73	15	empty

Compared structures

1XSC · Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant) in complex… · 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 0.89

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 1XSC · PDBe 1XSC · UniProt P50583

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