Structure of PDB 5g1z Chain A Binding Site BS03
Receptor Information
>5g1z Chain A (length=385) Species:
5855
(Plasmodium vivax) [
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IDYKFWYTQPVPKINDEFNESVNEPFISDNKVEDVRKDEYKLPPGYSWYV
CDVKDEKDRSEIYTLLTDNYVEDDDNIFRFNYSAEFLLWALTSPNYLKTW
HIGVKYDASNKLIGFISAIPTDICIHKRTIKMAEVNFLCVHKTLRSKRLA
PVLIKEITRRINLENIWQAIYTAGVYLPKPVSDARYYHRSINVKKLIEIG
FSSLNSRLTMSRAIKLYRVEDTLNIKNMRLMKKKDVEGVHKLLGSYLEQF
NLYAVFTKEEIAHWFLPIENVIYTYVNEENGKIKDMISFYSLPSQILGND
KYSTLNAAYSFYNVTTTATFKQLMQDAILLAKRNNFDVFNALEVMQNKSV
FEDLKFGEGDGSLKYYLYNWKCASFAPAHVGIVLL
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
5g1z Chain A Residue 1412 [
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Receptor-Ligand Complex Structure
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PDB
5g1z
Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.
Resolution
1.5 Å
Binding residue
(original residue number in PDB)
K172 L174
Binding residue
(residue number reindexed from 1)
K147 L149
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
N161 F162 L163 T197 L410
Catalytic site (residue number reindexed from 1)
N136 F137 L138 T172 L385
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:5g1z
,
PDBe:5g1z
,
PDBj:5g1z
PDBsum
5g1z
PubMed
28626547
UniProt
A5K1A2
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