1VHZ

Crystal structure of ADP compounds hydrolase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005829	cellular_component	cytosol
A	0006753	biological_process	nucleoside phosphate metabolic process
A	0016787	molecular_function	hydrolase activity
A	0019144	molecular_function	ADP-sugar diphosphatase activity
A	0019693	biological_process	ribose phosphate metabolic process
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0047631	molecular_function	ADP-ribose diphosphatase activity
B	0000287	molecular_function	magnesium ion binding
B	0005829	cellular_component	cytosol
B	0006753	biological_process	nucleoside phosphate metabolic process
B	0016787	molecular_function	hydrolase activity
B	0019144	molecular_function	ADP-sugar diphosphatase activity
B	0019693	biological_process	ribose phosphate metabolic process
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0047631	molecular_function	ADP-ribose diphosphatase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE APR A 197

Chain	Residue
A	ARG37
B	GLU141
B	PRO142
B	HOH252
B	HOH305
A	TYR39
A	GLU40
A	SER118
A	TYR119
A	HOH327
B	LEU21
B	VAL68
B	ASP140

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Functional Information from PROSITE/UniProt

site_id	PS00893
Number of Residues	22
Details	NUDIX_BOX Nudix box signature. GlidpgEsvyeAAnRELkEEvG

Chain	Residue	Details
A	GLY80-GLY101

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:16021622

Chain	Residue	Details
A	GLU40
A	SER118
B	GLU40
B	SER118

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLU95
A	GLU99
B	GLU95
B	GLU99

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