Structure of PDB 2ync Chain C Binding Site BS02
Receptor Information
>2ync Chain C (length=370) Species:
5855
(Plasmodium vivax) [
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DYKFWYTQPVPKINDEFNESVNEPFISDNKVEDVRKDEYKLPPGYSWYVC
DVKDEKDRSEIYTLLTDNYVEDDDNIFRFNYSAEFLLWALTSPNYLKTWH
IGVKYDASNKLIGFISAIPTDICIHKRTIKMAEVNFLCVHKTLRSKRLAP
VLIKEITRRINLENIWQAIYTAGVYLPKPVSDARYYHRSINVKKLIEIGF
LYKVEDTLNIKNMRLMKKKDVEGVHKLLGSYLEQFNLYAVFTKEEIAHWF
LPIENVIYTYVNEENGKIKDMISFYSLPSQILGNDKYSTLNAAYSFYNVT
TTATFKQLMQDAILLAKRNNFDVFNALEVMQNKSVFEDLKFGEGDGSLKY
YLYNWKCASFAPAHVGIVLL
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
2ync Chain C Residue 1411 [
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Receptor-Ligand Complex Structure
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PDB
2ync
Validation of N-Myristoyltransferase as an Antimalarial Drug Target Using an Integrated Chemical Biology Approach.
Resolution
1.75 Å
Binding residue
(original residue number in PDB)
S171 K172 L174
Binding residue
(residue number reindexed from 1)
S145 K146 L148
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
N161 F162 L163 T197 L410
Catalytic site (residue number reindexed from 1)
N135 F136 L137 T171 L370
Enzyme Commision number
2.3.1.97
: glycylpeptide N-tetradecanoyltransferase.
Gene Ontology
Molecular Function
GO:0004379
glycylpeptide N-tetradecanoyltransferase activity
GO:0016746
acyltransferase activity
GO:0046872
metal ion binding
Biological Process
GO:0006499
N-terminal protein myristoylation
GO:0018008
N-terminal peptidyl-glycine N-myristoylation
Cellular Component
GO:0005737
cytoplasm
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Biological Process
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Cellular Component
External links
PDB
RCSB:2ync
,
PDBe:2ync
,
PDBj:2ync
PDBsum
2ync
PubMed
24451586
UniProt
A5K1A2
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