1XSC

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004081	molecular_function	bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005759	cellular_component	mitochondrial matrix
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006167	biological_process	AMP biosynthetic process
A	0006754	biological_process	ATP biosynthetic process
A	0006915	biological_process	apoptotic process
A	0008796	molecular_function	bis(5'-nucleosyl)-tetraphosphatase activity
A	0008803	molecular_function	bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity
A	0016787	molecular_function	hydrolase activity
A	0034599	biological_process	cellular response to oxidative stress

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ATP A 154

Chain	Residue
A	HIS42
A	TYR87
A	ALA89
A	PHE133
A	GLU135

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	138
Details	Domain: {"description":"Nudix hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	21
Details	Motif: {"description":"Nudix box"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-1997","submissionDatabase":"UniProtKB","authors":["McLennan A.G."]}}]}

Chain

Residue

Details

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