2I5D

Crystal Structure of Human Inosine Triphosphate Pyrophosphatase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009117	biological_process	nucleotide metabolic process
A	0009143	biological_process	nucleoside triphosphate catabolic process
A	0009204	biological_process	deoxyribonucleoside triphosphate catabolic process
A	0016787	molecular_function	hydrolase activity
A	0035870	molecular_function	dITP diphosphatase activity
A	0036220	molecular_function	ITP diphosphatase activity
A	0036222	molecular_function	XTP diphosphatase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0047429	molecular_function	nucleoside triphosphate diphosphatase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17138556","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J4E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"HAMAP-Rule","id":"MF_03148","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}}]}

Chain

Residue

Details

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