Structure of PDB 2p6e Chain E

Receptor sequence
>2p6eE (length=443) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
DKAKKLENLLKLLQLNNDDTSKFTDHKFWRTQPVKDFDEKVVEEGPIDKP
KTPEDISDKPLPLLSSFEWCSIDVDNKKQLEDVFVLLNENYVEDRDAGFR
FNYTKEFFNWALKSPGWKKDWHIGVRVKETQKLVAFISAIPVTLGVRGKQ
VPSVEINFLCVHKQLRSKRLTPVLIKEITRRVNKCDIWHALYTAGIVLPA
PVSTCRYTHRPLNWKKLYEVDFTGLPDGHTEEDMIAENALPAKTKTAGLR
KLKKEDIDQVFELFKRYQSRFELIQIFTKEEFEHNFIGEESLPLDKQVIF
SYVVEQPDGKITDFFSFYSLPFTILNNTKYKDLGIGYLYYYATDADFQFK
DRFDPKATKALKTRLCELIYDACILAKNANMDVFNALTSQDNTLFLDDLK
FGPGDGFLNFYLFNYRAKPITGGLNPDNSNDIKRRSNVGVVML
3D structure
PDB2p6e Crystal structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoyl-CoA and inhibitors reveal the functional roles of the N-terminal region.
ChainE
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N169 F170 L171 T205 L455
Catalytic site (residue number reindexed from 1) N157 F158 L159 T193 L443
Enzyme Commision number 2.3.1.97: glycylpeptide N-tetradecanoyltransferase.
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 MYA E H38 W41 Y103 I168 N169 L171 V173 R178 S179 R181 T183 I187 T191 A202 T205 I208 L210 F425 H26 W29 Y91 I156 N157 L159 V161 R166 S167 R169 T171 I175 T179 A190 T193 I196 L198 F413
Gene Ontology
Molecular Function
GO:0004379 glycylpeptide N-tetradecanoyltransferase activity
GO:0016746 acyltransferase activity
Biological Process
GO:0006499 N-terminal protein myristoylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2p6e, PDBe:2p6e, PDBj:2p6e
PDBsum2p6e
PubMed17513302
UniProtP14743|NMT_YEAST Glycylpeptide N-tetradecanoyltransferase (Gene Name=NMT1)

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