Structure of PDB 1iyl Chain A

Receptor sequence
>1iylA (length=384) Species: 5476 (Candida albicans) [Search protein sequence]
TPEDVPNDPLPLISDFEWSTLDIDDNLQLDELYKLLYDNYVEDIDATFRF
KYSHEFFQWALKPPGWRKDWHVGVRVKSTGKLVAFIAATPVTFKLNKSNK
VIDSVEINFLCIHKKLRNKRLAPVLIKEITRRVNKQNIWQALYTGGSILP
TPLTTCRYQHRPINWSKLHDVGFSHLPPNQTKSSMVASYTLPNNPKLKGL
RPMTGKDVSTVLSLLYKYQERFDIVQLFTEEEFKHWMLGHDENSDSNVVK
SYVVEDENGIITDYFSYYLLPFTVLDNAQHDELGIAYLFYYASDSFEKPN
YKKRLNELITDALITSKKFGVDVFNCLTCQDNTYFLKDCKFGSGDGFLNY
YLFNYRTFPMDGGIDKKTKEVVEDQTSGIGVVLL
3D structure
PDB1iyl Crystal Structures of Candida albicans N-Myristoyltransferase with Two Distinct Inhibitors
ChainA
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N175 F176 L177 T211 L451
Catalytic site (residue number reindexed from 1) N108 F109 L110 T144 L384
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 R64 A Y107 D110 Y119 F176 Y225 H227 F240 F339 N392 C393 L451 Y40 D43 Y52 F109 Y158 H160 F173 F272 N325 C326 L384 PDBbind-CN: -logKd/Ki=9.00,IC50=1nM
BindingDB: IC50=1nM
Gene Ontology
Molecular Function
GO:0004379 glycylpeptide N-tetradecanoyltransferase activity
Biological Process
GO:0006499 N-terminal protein myristoylation

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Molecular Function
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Biological Process
External links
PDB RCSB:1iyl, PDBe:1iyl, PDBj:1iyl
PDBsum1iyl
PubMed12401496
UniProtP30418|NMT_CANAL Glycylpeptide N-tetradecanoyltransferase (Gene Name=NMT1)

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