8QNO

Crystal structure of S-adenosyl-L-homocysteine hydrolase treated at 368 K from Pyrococcus furiosus in complex with inosine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004013	molecular_function	adenosylhomocysteinase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006730	biological_process	one-carbon metabolic process
A	0016787	molecular_function	hydrolase activity
A	0033353	biological_process	S-adenosylmethionine cycle
A	0071269	biological_process	L-homocysteine biosynthetic process
B	0004013	molecular_function	adenosylhomocysteinase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006730	biological_process	one-carbon metabolic process
B	0016787	molecular_function	hydrolase activity
B	0033353	biological_process	S-adenosylmethionine cycle
B	0071269	biological_process	L-homocysteine biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00738
Number of Residues	15
Details	ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. ASNpLSTQDdVVAAL

Chain	Residue	Details
A	ALA78-LEU92

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site_id	PS00739
Number of Residues	17
Details	ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKnvvVvGYGwCGRGi.A

Chain	Residue	Details
A	GLY210-ALA226

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	34
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00563","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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