2WSL

Aged Form of Human Butyrylcholinesterase Inhibited by Tabun Analogue TA4

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A	CHOLINESTERASE	polymer	529	59745.6	1	UniProt (P06276) Pfam (PF00135) In PDB	HOMO SAPIENS (HUMAN)	BUTYRYLCHOLINESTERASE, ACYLCHOLINE ACYLHYDROLASE, CHOLINE ESTERASE II, BUTYRYLCHOLINE ESTERASE, PSEUDOCHOLINESTERASE
2	B	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose	branched		570.5	1	In PDB GlyTouCan (G28454KX)
3	C	alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose	branched		367.3	1	In PDB GlyTouCan (G86851RC)
4	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)
5	A	2-acetamido-2-deoxy-beta-D-glucopyranose	non-polymer		221.2	3	Chemie (NAG)
6	A	CHLORIDE ION	non-polymer		35.5	1	Chemie (CL)
7	A	SODIUM ION	non-polymer		23.0	1	Chemie (NA)
8	A	SULFATE ION	non-polymer		96.1	1	Chemie (SO4)
9	A	ETHYL DIHYDROGEN PHOSPHATE	non-polymer		126.0	1	Chemie (EFS)
10	A	FLUORIDE ION	non-polymer		19.0	1	Chemie (F)
11		water	water		18.0	397	Chemie (HOH)

Sequence modifications

A: 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	59745.6
Branched	Number of molecules	3
	Total formula weight	1508.4
Non-Polymers*	Number of molecules	8
	Total formula weight	963.2
All*	Total formula weight	62217.2

*Water molecules are not included.