Structure of PDB 1iyl Chain C

Receptor sequence
>1iylC (length=381) Species: 5476 (Candida albicans) [Search protein sequence]
DVPNDPLPLISDFEWSTLDIDDNLQLDELYKLLYDNYVEDIDATFRFKYS
HEFFQWALKPPGWRKDWHVGVRVKSTGKLVAFIAATPVTFKLNKSNKVID
SVEINFLCIHKKLRNKRLAPVLIKEITRRVNKQNIWQALYTGGSILPTPL
TTCRYQHRPINWSKLHDVGFSHLPPNQTKSSMVASYTLPNNPKLKGLRPM
TGKDVSTVLSLLYKYQERFDIVQLFTEEEFKHWMLGHDENSDSNVVKSYV
VEDENGIITDYFSYYLLPFTVLDNAQHDELGIAYLFYYASDSFEKPNYKK
RLNELITDALITSKKFGVDVFNCLTCQDNTYFLKDCKFGSGDGFLNYYLF
NYRTFPMDGGIDKKTKEVVEDQTSGIGVVLL
3D structure
PDB1iyl Crystal Structures of Candida albicans N-Myristoyltransferase with Two Distinct Inhibitors
ChainC
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) N175 F176 L177 T211 L451
Catalytic site (residue number reindexed from 1) N105 F106 L107 T141 L381
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 C Y107 I111 F117 Y119 F176 Y225 H227 F240 F339 N392 L394 L451 Y37 I41 F47 Y49 F106 Y155 H157 F170 F269 N322 L324 L381 BindingDB: IC50=1nM
Gene Ontology
Molecular Function
GO:0004379 glycylpeptide N-tetradecanoyltransferase activity
Biological Process
GO:0006499 N-terminal protein myristoylation

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

[Back to BioLiP]