2QZP

Crystal structure of mutation of an acylptide hydrolase/esterase from Aeropyrum pernix K1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0008236	molecular_function	serine-type peptidase activity
A	0008242	molecular_function	omega peptidase activity
A	0016787	molecular_function	hydrolase activity
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005737	cellular_component	cytoplasm
B	0006508	biological_process	proteolysis
B	0008236	molecular_function	serine-type peptidase activity
B	0008242	molecular_function	omega peptidase activity
B	0016787	molecular_function	hydrolase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Charge relay system => ECO:0000250

Chain	Residue	Details
A	SER445
A	ASP524
A	HIS556
B	SER445
B	ASP524
B	HIS556

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