Structure of PDB 6rua Chain B Binding Site BS01

Receptor Information

>6rua Chain B (length=526) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

IIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWS
DIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPK
PKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGF
LALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAAS
VSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCS
RENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMP
DILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEG
LKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPAL
EFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERR
DNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTL
NTESTRIMTKLRAQQCRFWTSFFPKV

Ligand information

Ligand ID

FUL

InChI

InChI=1S/C6H12O5/c1-2-3(7)4(8)5(9)6(10)11-2/h2-10H,1H3/t2-,3+,4+,5-,6-/m0/s1

InChIKey

SHZGCJCMOBCMKK-KGJVWPDLSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	C[C@H]1[C@H]([C@H]([C@@H]([C@H](O1)O)O)O)O
ACDLabs 10.04	OC1C(O)C(OC(O)C1O)C
CACTVS 3.341	C[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@@H]1O
OpenEye OEToolkits 1.5.0	CC1C(C(C(C(O1)O)O)O)O
CACTVS 3.341	C[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O

Formula

C6 H12 O5

Name

beta-L-fucopyranose;
beta-L-fucose;
6-deoxy-beta-L-galactopyranose;
L-fucose;
fucose;
6-DEOXY-BETA-L-GALACTOSE

PDB chain

6rua Chain I Residue 3 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	6rua Development of potent reversible selective inhibitors of butyrylcholinesterase as fluorescent probes.
Resolution	2.75 Å
Binding residue (original residue number in PDB)	N245 K248 F278
Binding residue (residue number reindexed from 1)	N242 K245 F275
Annotation score	1

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)	G113 G114 G146 S195 A196 Y234 V285 F287 E322 H435
Enzyme Commision number	3.1.1.8: cholinesterase.

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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Molecular Function

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Cellular Component

External links

PDB	RCSB:6rua, PDBe:6rua, PDBj:6rua
PDBsum	6rua
PubMed	31914836
UniProt	P06276\|CHLE_HUMAN Cholinesterase (Gene Name=BCHE)

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