8CG0

Crystal structure of S-adenosyl-L-homocysteine hydrolase from P. aeruginosa in complex with F2X-Entry library fragment H11

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
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
C	0004013	molecular_function	adenosylhomocysteinase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006730	biological_process	one-carbon metabolic process
C	0016787	molecular_function	hydrolase activity
C	0033353	biological_process	S-adenosylmethionine cycle
D	0004013	molecular_function	adenosylhomocysteinase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006730	biological_process	one-carbon metabolic process
D	0016787	molecular_function	hydrolase activity
D	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
A	SER84-ILE98

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

Chain	Residue	Details
A	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