7AMD

In situ assembly of choline acetyltransferase ligands by a hydrothiolation reaction reveals key determinants for inhibitor design

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A	Choline O-acetyltransferase	polymer	612	68113.4	1	UniProt (P28329) Pfam (PF00755) In PDB	Homo sapiens (Human)	Choline acetylase
2	A	[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(3~{R})-2,2-dimethyl-4-[[3-[2-[(1~{R})-2-(1-methylpyridin-4-yl)-1-naphthalen-1-yl-ethyl]sulfanylethylamino]-3-oxidanylidene-propyl]amino]-3-oxidanyl-4-oxidanylidene-butyl] hydrogen phosphate	non-polymer		1013.9	1	Chemie (RMW)
3	A	SODIUM ION	non-polymer		23.0	2	Chemie (NA)
4		water	water		18.0	210	Chemie (HOH)

Sequence modifications

A: 2 - 615 (UniProt: P28329)

PDB	External Database	Details
Ala 1	-	expression tag
Ala 225	Glu 343	engineered mutation
Ala 226	Asp 344	engineered mutation
Ala 227	Glu 345	engineered mutation
Met 343	Val 461	conflict
Pro 349	Ser 464	conflict
-	Ser 465	deletion
-	Arg 466	deletion
Glu 350	Lys 467	conflict
Val 352	Ile 469	conflict
Ser 354	Ala 471	conflict
Pro 355	Asp 472	conflict
Met 356	Ser 473	conflict
Pro 358	Ser 475	conflict
-	Glu 476	deletion
Ala 518	Lys 636	engineered mutation
Ala 519	Glu 637	engineered mutation
Ala 582	Lys 700	engineered mutation
Ala 583	Glu 701	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	1
	Total formula weight	68113.4
Non-Polymers*	Number of molecules	3
	Total formula weight	1059.8
All*	Total formula weight	69173.2

*Water molecules are not included.