Structure of PDB 5a27 Chain A

Receptor sequence

>5a27A (length=411) Species: 5664 (Leishmania major)

AHAFWSTQPVPQTEDETEKIVFAGPMDEPKTVADIPEEPYPIASTFEWWT
PNMEAADDIHAIYELLRDNYVEDDDSMFRFNYSEEFLQWALCPPNYIPDW
HVAVRRKADKKLLAFIAGVPVTLRMGTPKYMKVKAQEKGEGEEAAKYDEP
RHICEINFLCVHKQLREKRLAPILIKEATRRVNRTNVWQAVYTAGVLLPT
PYASGQYFHRSLNPEKLVEIRFSGIPAQYQKFQNPMAMLKRNYQLPSAPK
NSGLREMKPSDVPQVRRILMNYLDSFDVGPVFSDAEISHYLLPRDGVVFT
YVVENDKKVTDFFSFYRIPSTVIGNSNYNLLNAAYVHYYAATSIPLHQLI
LDLLIVAHSRGFDVCNMVEILDNRSFVEQLKFGAGDGHLRYYFYNWAYPK
IKPSQVALVML

3D structure

• PDB: 5a27 Discovery of High Affinity Inhibitors of Leishmania Donovani N-Myristoyltransferase.
• Chain: A
• Resolution: 1.37 Å

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 A13 F14 W15 Y80 V81 L169 C170 V171 R176 E177 R179 A181 P182 T189 V192 A200 Y202 T203 L208 Y404	H2 A3 F4 W5 Y70 V71 L159 C160 V161 R166 E167 R169 A171 P172 T179 V182 A190 Y192 T193 L198 Y394
BS02	TUT	A	V81 E82 F88 F90 Y92 Y217 F218 F232 Y345 M377 M420 L421	V71 E72 F78 F80 Y82 Y207 F208 F222 Y335 M367 M410 L411	MOAD: Ki=0.02uM
BS03	MG	A	L175 K178 L180	L165 K168 L170

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

External links

• PDB: RCSB:5a27, PDBe:5a27, PDBj:5a27
• PDBsum: 5a27
• PubMed: 26962429
• UniProt: Q4Q5S8