8AJU

Crystal structure of the Q65A mutant of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa cocrystallized with adenosine in the presence of K+ cations

This is a non-PDB format compatible entry.

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
AAA	0071269	biological_process	L-homocysteine biosynthetic process
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
CCC	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. SCNiFSTQDqAAAAI

Chain	Residue	Details
AAA	SER84-ILE98

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00563","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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