Structure of PDB 4caf Chain A

Receptor sequence
>4cafA (length=384) Species: 5855 (Plasmodium vivax) [Search protein sequence]
DYKFWYTQPVPKINDEFNESVNEPFISDNKVEDVRKDEYKLPPGYSWYVC
DVKDEKDRSEIYTLLTDNYVEDDDNIFRFNYSAEFLLWALTSPNYLKTWH
IGVKYDASNKLIGFISAIPTDICIHKRTIKMAEVNFLCVHKTLRSKRLAP
VLIKEITRRINLENIWQAIYTAGVYLPKPVSDARYYHRSINVKKLIEIGF
SSLNSRLTMSRAIKLYRVEDTLNIKNMRLMKKKDVEGVHKLLGSYLEQFN
LYAVFTKEEIAHWFLPIENVIYTYVNEENGKIKDMISFYSLPSQILGNDK
YSTLNAAYSFYNVTTTATFKQLMQDAILLAKRNNFDVFNALEVMQNKSVF
EDLKFGEGDGSLKYYLYNWKCASFAPAHVGIVLL
3D structure
PDB4caf Design and Synthesis of High Affinity Inhibitors of Plasmodium Falciparum and Plasmodium Vivax N-Myristoyltransferases Directed by Ligand Efficiency Dependent Lipophilicity (Lelp).
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 L384
Enzyme Commision number 2.3.1.97: glycylpeptide N-tetradecanoyltransferase.
Interaction with ligand
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4caf, PDBe:4caf, PDBj:4caf
PDBsum4caf
PubMed24641010
UniProtA5K1A2

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