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1Q6X

Crystal structure of rat choline acetyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0001547biological_processantral ovarian follicle growth
A0001666biological_processresponse to hypoxia
A0004102molecular_functioncholine O-acetyltransferase activity
A0005737cellular_componentcytoplasm
A0007268biological_processchemical synaptic transmission
A0007274biological_processneuromuscular synaptic transmission
A0007517biological_processmuscle organ development
A0007529biological_processestablishment of synaptic specificity at neuromuscular junction
A0007584biological_processresponse to nutrient
A0007613biological_processmemory
A0007622biological_processrhythmic behavior
A0007628biological_processadult walking behavior
A0008292biological_processacetylcholine biosynthetic process
A0008374molecular_functionO-acyltransferase activity
A0009410biological_processresponse to xenobiotic stimulus
A0016358biological_processdendrite development
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0030182biological_processneuron differentiation
A0030424cellular_componentaxon
A0033265molecular_functioncholine binding
A0043005cellular_componentneuron projection
A0043025cellular_componentneuronal cell body
A0043179biological_processrhythmic excitation
A0045202cellular_componentsynapse
A0045471biological_processresponse to ethanol
B0001547biological_processantral ovarian follicle growth
B0001666biological_processresponse to hypoxia
B0004102molecular_functioncholine O-acetyltransferase activity
B0005737cellular_componentcytoplasm
B0007268biological_processchemical synaptic transmission
B0007274biological_processneuromuscular synaptic transmission
B0007517biological_processmuscle organ development
B0007529biological_processestablishment of synaptic specificity at neuromuscular junction
B0007584biological_processresponse to nutrient
B0007613biological_processmemory
B0007622biological_processrhythmic behavior
B0007628biological_processadult walking behavior
B0008292biological_processacetylcholine biosynthetic process
B0008374molecular_functionO-acyltransferase activity
B0009410biological_processresponse to xenobiotic stimulus
B0016358biological_processdendrite development
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0030182biological_processneuron differentiation
B0030424cellular_componentaxon
B0033265molecular_functioncholine binding
B0043005cellular_componentneuron projection
B0043025cellular_componentneuronal cell body
B0043179biological_processrhythmic excitation
B0045202cellular_componentsynapse
B0045471biological_processresponse to ethanol
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 1001
ChainResidue
BPHE588
BHIS589
BCYS591
BTHR594
BHOH1018
BHOH1045

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1002
ChainResidue
ATHR594
AHOH1047
AHOH1096
APHE588
AHIS589
ACYS591

Functional Information from PROSITE/UniProt
site_idPS00439
Number of Residues16
DetailsACYLTRANSF_C_1 Acyltransferases ChoActase / COT / CPT family signature 1. LPkLPVPpLqQTLatY
ChainResidueDetails
ALEU23-TYR38

site_idPS00440
Number of Residues28
DetailsACYLTRANSF_C_2 Acyltransferases ChoActase / COT / CPT family signature 2. RWyDKsLqFVvgrDGtcgvvcEHspfDG
ChainResidueDetails
AARG312-GLY339

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS334
BHIS334

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AGLY412
BGLY412

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER450
AGLN551
BSER450
BGLN551

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER17
ASER365
BSER17
BSER365

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 605
ChainResidueDetails
ATYR95
APRO108
AHIS334
ASER550

site_idMCSA2
Number of Residues4
DetailsM-CSA 605
ChainResidueDetails
BTYR95
BPRO108
BHIS334
BSER550

218853

PDB entries from 2024-04-24

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