Structure of PDB 4b12 Chain B

Receptor sequence
>4b12B (length=385) Species: 5855 (Plasmodium vivax) [Search protein sequence]
MDYKFWYTQPVPKINDEFNESVNEPFISDNKVEDVRKDEYKLPPGYSWYV
CDVKDEKDRSEIYTLLTDNYVEDDDNIFRFNYSAEFLLWALTSPNYLKTW
HIGVKYDASNKLIGFISAIPTDICIHKRTIKMAEVNFLCVHKTLRSKRLA
PVLIKEITRRINLENIWQAIYTAGVYLPKPVSDARYYHRSINVKKLIEIG
FSSLNSRLTMSRAIKLYRVEDTLNIKNMRLMKKKDVEGVHKLLGSYLEQF
NLYAVFTKEEIAHWFLPIENVIYTYVNEENGKIKDMISFYSLPSQILGND
KYSTLNAAYSFYNVTTTATFKQLMQDAILLAKRNNFDVFNALEVMQNKSV
FEDLKFGEGDGSLKYYLYNWKCASFAPAHVGIVLL
3D structure
PDB4b12 Design and Synthesis of Inhibitors of Plasmodium Falciparum N-Myristoyltransferase, a Promising Target for Anti-Malarial Drug Discovery.
ChainB
Resolution1.79 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) N136 F137 L138 T172 L385
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:4b12, PDBe:4b12, PDBj:4b12
PDBsum4b12
PubMed23035716
UniProtA5K1A2

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