8AI7

Structure of carbamoylated human butyrylcholinesterase upon reaction with 3-(((2-cycloheptylethyl)(methyl)amino)methyl)-1H-indol-7-yl N,N-dimethylcarbamate

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A (F)	Cholinesterase	polymer	529	59784.6	1	UniProt (P06276) Pfam (PF00135)	Homo sapiens (human)	Acylcholine acylhydrolase,Butyrylcholine esterase,Choline esterase II,Pseudocholinesterase
2	B, C, E (B, C, E)	alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose	branched		367.3	3	In PDB GlyTouCan (G86851RC)
3	D (D)	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose	branched		570.5	1	In PDB GlyTouCan (G21290RB)
4	F, G, H (F)	SULFATE ION	non-polymer		96.1	3	Chemie (SO4)
5	I, J, K, L, M... (F)	CHLORIDE ION	non-polymer		35.5	7	Chemie (CL)
6	P (F)	SODIUM ION	non-polymer		23.0	1	Chemie (NA)
7	Q (F)	3-[[2-cycloheptylethyl(methyl)amino]methyl]-1~{H}-indol-7-ol	non-polymer		300.4	1	Chemie (M8X)
8	R, S (F)	2-acetamido-2-deoxy-beta-D-glucopyranose	non-polymer		221.2	2	Chemie (NAG)
9	T, U, V, W (F)	GLYCEROL	non-polymer		92.1	4	Chemie (GOL)
10	X (F)	water	water		18.0	202	Chemie (HOH)

Sequence modifications

F: 1 - 529 (UniProt: P06276)

PDB	External Database	Details
Gln 17	Asn 45	engineered mutation
Gln 455	Asn 483	engineered mutation
Gln 481	Asn 509	engineered mutation
Gln 486	Asn 514	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	1
	Total formula weight	59784.6
Branched	Number of molecules	4
	Total formula weight	1672.6
Non-Polymers*	Number of molecules	18
	Total formula weight	1670.6
All*	Total formula weight	63127.8

*Water molecules are not included.