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2FY2

Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1ACholine O-acetyltransferasepolymer61268113.41UniProt (P28329)
Pfam (PF00755)
In PDB
Homo sapiens (human)CHOACTase, Choline acetylase, ChAT
2waterwater18.0544Chemie (HOH)
Sequence modifications
A: 2 - 615 (UniProt: P28329)
PDBExternal DatabaseDetails
Ala 1-cloning artifact
Ala 225Glu 343engineered mutation
Ala 226Asp 344engineered mutation
Ala 227Glu 345engineered mutation
-Ser 464SEE REMARK 999
-Ser 465SEE REMARK 999
Pro 346Arg 466SEE REMARK 999
Glu 349Lys 467SEE REMARK 999
Val 351Ile 469SEE REMARK 999
Ser 353Ala 471SEE REMARK 999
Pro 354Asp 472SEE REMARK 999
Met 355Ser 473SEE REMARK 999
-Ser 475SEE REMARK 999
Pro 357Glu 476SEE REMARK 999
Ala 518Lys 636engineered mutation
Ala 519Glu 637engineered mutation
Ala 582Lys 700engineered mutation
Ala 583Glu 701engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains1
Total formula weight68113.4
All*Total formula weight68113.4
*Water molecules are not included.

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PDB entries from 2024-04-24

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