8AJW

Crystal structure of the Q65N mutant of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa cocrystallized with adenosine in the presence of K+ cations

Functional Information from GO Data

Chain	GOid	namespace	contents
AAA	0004013	molecular_function	adenosylhomocysteinase activity
AAA	0005737	cellular_component	cytoplasm
AAA	0005829	cellular_component	cytosol
AAA	0006730	biological_process	one-carbon metabolic process
AAA	0016787	molecular_function	hydrolase activity
AAA	0033353	biological_process	S-adenosylmethionine cycle
BBB	0004013	molecular_function	adenosylhomocysteinase activity
BBB	0005737	cellular_component	cytoplasm
BBB	0005829	cellular_component	cytosol
BBB	0006730	biological_process	one-carbon metabolic process
BBB	0016787	molecular_function	hydrolase activity
BBB	0033353	biological_process	S-adenosylmethionine cycle
CCC	0004013	molecular_function	adenosylhomocysteinase activity
CCC	0005737	cellular_component	cytoplasm
CCC	0005829	cellular_component	cytosol
CCC	0006730	biological_process	one-carbon metabolic process
CCC	0016787	molecular_function	hydrolase activity
CCC	0033353	biological_process	S-adenosylmethionine cycle
DDD	0004013	molecular_function	adenosylhomocysteinase activity
DDD	0005737	cellular_component	cytoplasm
DDD	0005829	cellular_component	cytosol
DDD	0006730	biological_process	one-carbon metabolic process
DDD	0016787	molecular_function	hydrolase activity
DDD	0033353	biological_process	S-adenosylmethionine cycle

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
AAA	SER84-ILE98

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

Chain	Residue	Details
AAA	GLY221-SER237

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00563