Structure of PDB 2fy4 Chain A

Receptor sequence
>2fy4A (length=589) Species: 9606 (Homo sapiens) [Search protein sequence]
SGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGET
LQQKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFPGT
DDQLRFAASLISGVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFS
SYRLPGHTQDTLVAQMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQ
LRKIVKMASNAAARLPPIGLLTSDGRSEWAEARTVLVKDSTNRDSLDMIE
RCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANRWYDKSLQFVVGR
DGTCGVVCEHSPFDGIVLVQCTEHLLKHMTQPELVRSPMVPLPAPRRLRW
KCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFI
QVALQLAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVT
DHKAAVPASEKLLLLKDAIRAQTAYTVMAITGMAIDNHLLALRELARAMC
AALPEMFMDETYLMSNRFVLSTSQVPTTTEMFCCYGPVVPNGYGACYNPQ
PETILFCISSFHSCAATSSSKFAKAVEESLIDMRDLCSL
3D structure
PDB2fy4 Substrate binding and catalytic mechanism of human choline acetyltransferase.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y85 P98 H324 S540
Catalytic site (residue number reindexed from 1) Y75 P88 H310 S523
Enzyme Commision number 2.3.1.6: choline O-acetyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 COA A G143 Q144 D328 I330 K407 K410 S412 P413 D414 S438 A439 S440 Q541 G133 Q134 D314 I316 K390 K393 S395 P396 D397 S421 A422 S423 Q524 BindingDB: Ki=75000nM
Gene Ontology
Molecular Function
GO:0016746 acyltransferase activity

View graph for
Molecular Function
External links
PDB RCSB:2fy4, PDBe:2fy4, PDBj:2fy4
PDBsum2fy4
PubMed17144655
UniProtP28329|CLAT_HUMAN Choline O-acetyltransferase (Gene Name=CHAT)

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