MolNFT v1 · #27728 · protein

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

1XSC · BIS(5'-nucleosyl)-tetraphosphatase: “Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant) in complex with ATP”. Solution nmr, 1 ligand (ATP), 2 pockets (best druggability 0.38). MolNFT v1 #27728 on GenesisL1…

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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