3MIL

Crystal structure of isoamyl acetate-hydrolyzing esterase from Saccharomyces cerevisiae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005575	cellular_component	cellular_component
A	0006083	biological_process	acetate metabolic process
A	0006629	biological_process	lipid metabolic process
A	0016042	biological_process	lipid catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0005575	cellular_component	cellular_component
B	0006083	biological_process	acetate metabolic process
B	0006629	biological_process	lipid metabolic process
B	0016042	biological_process	lipid catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016788	molecular_function	hydrolase activity, acting on ester bonds

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 241

Chain	Residue
A	SER12
A	LYS52
A	GLY53
A	ASN83
A	GLN91
A	ARG143
A	HIS190
A	HOH637

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 241

Chain	Residue
B	LYS52
B	GLY53
B	ASN83
B	GLN91
B	TRP129
B	ARG143
B	HIS190
B	HOH430
B	SER12

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:21069734

Chain	Residue	Details
A	SER12
B	SER12

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:21069734

Chain	Residue	Details
A	ASP187
B	ASP187

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:21069734

Chain	Residue	Details
A	HIS190
B	HIS190

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000305|PubMed:21069734

Chain	Residue	Details
A	GLY53
A	ASN83
B	GLY53
B	ASN83

---