5YDH

Crystal structure of acetylcholinesterase catalytic subunits of the malaria vector anopheles gambiae, 3.2 A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004104	molecular_function	cholinesterase activity
B	0004104	molecular_function	cholinesterase activity

Functional Information from PROSITE/UniProt

site_id	PS00122
Number of Residues	16
Details	CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpsrVtLfGeSAG

Chain	Residue	Details
A	PHE347-GLY362

---

site_id	PS00941
Number of Residues	11
Details	CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYINVVaP

Chain	Residue	Details
A	GLU253-PRO263

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10039

Chain	Residue	Details
A	SER360
B	SER360

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Charge relay system => ECO:0000250

Chain	Residue	Details
A	GLU486
A	HIS600
B	GLU486
B	HIS600

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN220
A	ASN670
B	ASN220
B	ASN670

---