2ZTI

Structures of dimeric nonstandard nucleotide triphosphate pyrophosphatase from Pyrococcus horikoshii OT3: functional significance of interprotomer conformational changes

Replaces:  2EHK

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005737	cellular_component	cytoplasm
A	0009117	biological_process	nucleotide metabolic process
A	0009143	biological_process	nucleoside triphosphate catabolic process
A	0009146	biological_process	purine nucleoside triphosphate catabolic process
A	0016787	molecular_function	hydrolase activity
A	0017111	molecular_function	ribonucleoside triphosphate phosphatase activity
A	0035870	molecular_function	dITP diphosphatase activity
A	0036220	molecular_function	ITP diphosphatase activity
A	0036222	molecular_function	XTP diphosphatase activity
A	0046872	molecular_function	metal ion binding
A	0047429	molecular_function	nucleoside triphosphate diphosphatase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 187

Chain	Residue
A	GLU36
A	ASP65
A	HOH189
A	HOH243
A	HOH259
A	HOH260

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01405

Chain	Residue	Details
A	ASP65

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:18062990, ECO:0000269|Ref.2, ECO:0007744|PDB:2DVO, ECO:0007744|PDB:2E5X

Chain	Residue	Details
A	THR7
A	SER66
A	PHE140
A	LYS163
A	HIS168

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:18062990, ECO:0007744|PDB:2ZTI

Chain	Residue	Details
A	GLU36
A	ASP65

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