Structure of PDB 6ary Chain B

Receptor sequence
>6aryB (length=537) Species: 7165 (Anopheles gambiae) [Search protein sequence]
NDPLVVNTDKGRIRGITVDAPSGKKVDVWLGIPYAQPPVGPLRFRHPRPA
EKWTGVLNTTTPPNSCVQIVDTVFGDFPGATMWNPNTPLSEDCLYINVVA
PRPRPKNAAVMLWIFGGSFYSGTATLDVYDHRALASEENVIVVSLQYRVA
SLGFLFLGTPEAPGNAGLFDQNLALRWVRDNIHRFGGDPSRVTLFGESAG
AVSVSLHLLSALSRDLFQRAILQSGSPTAPWALVSREEATLRALRLAEAV
GCPHEPSKLSDAVECLRGKDPHVLVNNEWGTLGICEFPFVPVVDGAFLDE
TPQRSLASGRFKKTEILTGSNTEEGYYFIIYYLTELLRKEEGVTVTREEF
LQAVRELNPYVNGAARQAIVFEYTDWTEPDNPNSNRDALDKMVGDYHFTC
NVNEFAQRYAEEGNNVYMYLYTHRSKGNPWPRWTGVMHGDEINYVFGEPL
NPTLGYTEDEKDFSRKIMRYWSNFAKTGNPNPNTASSEFPEWPKHTAHGR
HYLELGLNTSFVGRGPRLRQCAFWKKYLPQLVAATSN
3D structure
PDB6ary Structure of the G119S Mutant Acetylcholinesterase of the Malaria Vector Anopheles gambiae Reveals Basis of Insecticide Resistance.
ChainB
Resolution2.257 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G279 S280 S360 A361 E486 H600
Catalytic site (residue number reindexed from 1) G117 S118 S198 A199 E324 H438
Enzyme Commision number 3.1.1.7: acetylcholinesterase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 BT7 B W245 G278 G279 S280 S360 A361 W393 Y489 F490 H600 W83 G116 G117 S118 S198 A199 W231 Y327 F328 H438
Gene Ontology
Molecular Function
GO:0004104 cholinesterase activity

View graph for
Molecular Function
External links
PDB RCSB:6ary, PDBe:6ary, PDBj:6ary
PDBsum6ary
PubMed29276037
UniProtQ869C3|ACES_ANOGA Acetylcholinesterase (Gene Name=Ace)

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