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1XSC

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004081molecular_functionbis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005759cellular_componentmitochondrial matrix
A0006139biological_processnucleobase-containing compound metabolic process
A0006167biological_processAMP biosynthetic process
A0006754biological_processATP biosynthetic process
A0006915biological_processapoptotic process
A0008796molecular_functionbis(5'-nucleosyl)-tetraphosphatase activity
A0008803molecular_functionbis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity
A0016787molecular_functionhydrolase activity
A0034599biological_processcellular response to oxidative stress
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ATP A 154
ChainResidue
AHIS42
ATYR87
AALA89
APHE133
AGLU135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.5
ChainResidueDetails
ALEU8

226707

PDB entries from 2024-10-30

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