Structure of PDB 1iyl Chain B

Receptor sequence
>1iylB (length=380) Species: 5476 (Candida albicans) [Search protein sequence]
VPNDPLPLISDFEWSTLDIDDNLQLDELYKLLYDNYVEDIDATFRFKYSH
EFFQWALKPPGWRKDWHVGVRVKSTGKLVAFIAATPVTFKLNKSNKVIDS
VEINFLCIHKKLRNKRLAPVLIKEITRRVNKQNIWQALYTGGSILPTPLT
TCRYQHRPINWSKLHDVGFSHLPPNQTKSSMVASYTLPNNPKLKGLRPMT
GKDVSTVLSLLYKYQERFDIVQLFTEEEFKHWMLGHDENSDSNVVKSYVV
EDENGIITDYFSYYLLPFTVLDNAQHDELGIAYLFYYASDSFEKPNYKKR
LNELITDALITSKKFGVDVFNCLTCQDNTYFLKDCKFGSGDGFLNYYLFN
YRTFPMDGGIDKKTKEVVEDQTSGIGVVLL
3D structure
PDB1iyl Crystal Structures of Candida albicans N-Myristoyltransferase with Two Distinct Inhibitors
ChainB
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) N104 F105 L106 T140 L380
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 B Y107 F117 Y119 N175 F176 Y225 H227 F240 F339 I352 Y354 N392 L451 Y36 F46 Y48 N104 F105 Y154 H156 F169 F268 I281 Y283 N321 L380 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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