Structure of PDB 5ydj Chain B

Receptor sequence
>5ydjB (length=538) Species: 7165 (Anopheles gambiae) [Search protein sequence]
DNDPLVVNTDKGRIRGITVDAPSGKKVDVWLGIPYAQPPVGPLRFRHPRP
AEKWTGVLNTTTPPNSCVQIVDTVFGDFPGATMWNPNTPLSEDCLYINVV
APRPRPKNAAVMLWIFGGGFYSGTATLDVYDHRALASEENVIVVSLQYRV
ASLGFLFLGTPEAPGNAGLFDQNLALRWVRDNIHRFGGDPSRVTLFGESA
GAVSVSLHLLSALSRDLFQRAILQSGSPTAPWALVSREEATLRALRLAEA
VGCPHEPSKLSDAVECLRGKDPHVLVNNEWGTLGICEFPFVPVVDGAFLD
ETPQRSLASGRFKKTEILTGSNTEEGYYFIIYYLTELLRKEEGVTVTREE
FLQAVRELNPYVNGAARQAIVFEYTDWTEPDNPNSNRDALDKMVGDYHFT
CNVNEFAQRYAEEGNNVYMYLYTHRSKGNPWPRWTGVMHGDEINYVFGEP
LNPTLGYTEDEKDFSRKIMRYWSNFAKTGNPNPNTASSEFPEWPKHTAHG
RHYLELGLNTSFVGRGPRLRQCAFWKKYLPQLVAATSN
3D structure
PDB5ydj Crystal structures of acetylcholinesterase of the malaria vector Anopheles gambiae reveal a polymerization interface, ligand binding residues and post translational modifications
ChainB
Resolution3.04 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 G280 S360 A361 E486 H600
Catalytic site (residue number reindexed from 1) G118 G119 S199 A200 E325 H439
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 CO B E410 H416 E249 H255
Gene Ontology
Molecular Function
GO:0004104 cholinesterase activity

View graph for
Molecular Function
External links
PDB RCSB:5ydj, PDBe:5ydj, PDBj:5ydj
PDBsum5ydj
PubMed
UniProtQ869C3|ACES_ANOGA Acetylcholinesterase (Gene Name=Ace)

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