Structure of PDB 4xii Chain A

Receptor sequence
>4xiiA (length=527) Species: 9606 (Homo sapiens) [Search protein sequence]
DIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKW
SDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAP
KPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG
FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAA
SVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGC
SRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDM
PDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQE
GLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPA
LEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER
RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLT
LNTESTRIMTKLRAQQCRFWTSFFPKV
3D structure
PDB4xii Structure-based development of nitroxoline derivatives as potential multifunctional anti-Alzheimer agents.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G116 G117 G149 S198 A199 Y237 V288 F290 E325 H438
Catalytic site (residue number reindexed from 1) G114 G115 G147 S196 A197 Y235 V286 F288 E323 H436
Enzyme Commision number 3.1.1.8: cholinesterase.
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 40V A N68 I69 D70 W82 G116 G117 E197 S198 W231 F329 Y332 H438 N66 I67 D68 W80 G114 G115 E195 S196 W229 F327 Y330 H436 PDBbind-CN: -logKd/Ki=6.60,Kd=0.25uM
BindingDB: IC50=215nM
BS02 FUL A N245 F278 N243 F276
BS03 FUL A S487 T488 S485 T486
Gene Ontology
Molecular Function
GO:0001540 amyloid-beta binding
GO:0003824 catalytic activity
GO:0003990 acetylcholinesterase activity
GO:0004104 cholinesterase activity
GO:0005515 protein binding
GO:0016788 hydrolase activity, acting on ester bonds
GO:0019899 enzyme binding
GO:0033265 choline binding
GO:0042802 identical protein binding
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0006581 acetylcholine catabolic process
GO:0006805 xenobiotic metabolic process
GO:0007584 response to nutrient
GO:0007612 learning
GO:0008285 negative regulation of cell population proliferation
GO:0009410 response to xenobiotic stimulus
GO:0014016 neuroblast differentiation
GO:0016486 peptide hormone processing
GO:0019695 choline metabolic process
GO:0043279 response to alkaloid
GO:0050783 cocaine metabolic process
GO:0050805 negative regulation of synaptic transmission
GO:0051384 response to glucocorticoid
GO:0051593 response to folic acid
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005641 nuclear envelope lumen
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0005886 plasma membrane
GO:0072562 blood microparticle

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Biological Process
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Cellular Component
External links
PDB RCSB:4xii, PDBe:4xii, PDBj:4xii
PDBsum4xii
PubMed26116179
UniProtP06276|CHLE_HUMAN Cholinesterase (Gene Name=BCHE)

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