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2FY4

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0016746molecular_functionacyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE COA A 2000
ChainResidue
AGLY143
ASER412
APRO413
AASP414
AGLU437
ASER438
AALA439
ASER440
AILE452
ATHR493
AGLN541
AGLN144
AHOH2358
AHOH2442
AHOH2444
AHIS324
AASP328
AGLY329
AILE330
ALYS407
ALYS410
ACYS411

Functional Information from PROSITE/UniProt
site_idPS00439
Number of Residues16
DetailsACYLTRANSF_C_1 Acyltransferases ChoActase / COT / CPT family signature 1. LPkLPVPpLqQTLatY
ChainResidueDetails
ALEU13-TYR28

site_idPS00440
Number of Residues28
DetailsACYLTRANSF_C_2 Acyltransferases ChoActase / COT / CPT family signature 2. RWyDKsLqFVvgrDGtcgvvcEHspfDG
ChainResidueDetails
AARG302-GLY329

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS324

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
APHE405
AARG443
ATHR544

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P32738
ChainResidueDetails
ASER7
APRO357

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q6x
ChainResidueDetails
APRO98
ATYR85
ASER540
AHIS324

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1q6x
ChainResidueDetails
ASER540
AHIS324

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PDB entries from 2024-09-11

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