Structure of PDB 3h5z Chain A

Receptor sequence
>3h5zA (length=411) Species: 5664 (Leishmania major) [Search protein sequence]
AHAFWSTQPVPQTEDETEKIVFAGPMDEPKTVADIPEEPYPIASTFEWWT
PNMEAADDIHAIYELLRDNYVEDDDSMFRFNYSEEFLQWALCPPNYIPDW
HVAVRRKADKKLLAFIAGVPVTLRMGTPKYMKVKAQEKGEGEEAAKYDEP
RHICEINFLCVHKQLREKRLAPILIKEATRRVNRTNVWQAVYTAGVLLPT
PYASGQYFHRSLNPEKLVEIRFSGIPAQYQKFQNPMAMLKRNYQLPSAPK
NSGLREMKPSDVPQVRRILMNYLDSFDVGPVFSDAEISHYLLPRDGVVFT
YVVENDKKVTDFFSFYRIPSTVIGNSNYNLLNAAYVHYYAATSIPLHQLI
LDLLIVAHSRGFDVCNMVEILDNRSFVEQLKFGAGDGHLRYYFYNWAYPK
IKPSQVALVML
3D structure
PDB3h5z N-myristoyltransferase inhibitors as new leads to treat sleeping sickness.
ChainA
Resolution1.49 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N167 F168 L169 T203 L421
Catalytic site (residue number reindexed from 1) N157 F158 L159 T193 L411
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 MYA A H12 F14 W15 Y80 V81 I166 L169 C170 V171 R176 E177 R179 A181 P182 V192 A200 Y202 T203 L208 Y404 H2 F4 W5 Y70 V71 I156 L159 C160 V161 R166 E167 R169 A171 P172 V182 A190 Y192 T193 L198 Y394
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
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:3h5z, PDBe:3h5z, PDBj:3h5z
PDBsum3h5z
PubMed20360736
UniProtQ4Q5S8

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