Structure of PDB 2w6c Chain X

Receptor sequence

>2w6cX (length=528) Species: 7787 (Tetronarce californica)

SELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKP
WSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPS
PRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAF
GFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGG
ASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELGRNLN
CNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPT
SLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFM
SGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICP
LMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLV
KELNYTAEEEALSRRIMHYWATFAKTGNPNEPSKWPLFTTKEQKFIDLNT
EPMKVHQRLRVQMCVFWNQFLPKLLNAT

3D structure

• PDB: 2w6c The Crystal Structure of a Complex of Acetylcholinesterase with a Bis-(-)-Nor-Meptazinol Derivative Reveals Disruption of the Catalytic Triad.
• Chain: X
• Resolution: 2.69 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G118 G119 S200 A201 H440
• Catalytic site (residue number reindexed from 1): G115 G116 S197 A198 H437
• 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	BM4	X	W84 G118 Y121 S200 F330 Y334 H440	W81 G115 Y118 S197 F327 Y331 H437	PDBbind-CN: -logKd/Ki=8.41,IC50=3.9nM

Gene Ontology

Molecular Function

• GO:0003990 acetylcholinesterase activity
• GO:0004104 cholinesterase activity

Biological Process

• GO:0001507 acetylcholine catabolic process in synaptic cleft

External links

• PDB: RCSB:2w6c, PDBe:2w6c, PDBj:2w6c
• PDBsum: 2w6c
• PubMed: 19326912
• UniProt: P04058|ACES_TETCF Acetylcholinesterase (Gene Name=ache)