Structure of PDB 4cyn Chain A

Receptor sequence

>4cynA (length=411) Species: 5664 (Leishmania major)

AHAFWSTQPVPQTEDETEKIVFAGPMDEPKTVADIPEEPYPIASTFEWWT
PNMEAADDIHAIYELLRDNYVEDDDSMFRFNYSEEFLQWALCPPNYIPDW
HVAVRRKADKKLLAFIAGVPVTLRMGTPKYMKVKAQEKGEGEEAAKYDEP
RHICEINFLCVHKQLREKRLAPILIKEATRRVNRTNVWQAVYTAGVLLPT
PYASGQYFHRSLNPEKLVEIRFSGIPAQYQKFQNPMAMLKRNYQLPSAPK
NSGLREMKPSDVPQVRRILMNYLDSFDVGPVFSDAEISHYLLPRDGVVFT
YVVENDKKVTDFFSFYRIPSTVIGNSNYNLLNAAYVHYYAATSIPLHQLI
LDLLIVAHSRGFDVCNMVEILDNRSFVEQLKFGAGDGHLRYYFYNWAYPK
IKPSQVALVML

3D structure

• PDB: 4cyn Structure-Based Design of Potent and Selective Leishmania N- Myristoyltransferase Inhibitors.
• Chain: A
• Resolution: 1.4 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	MG	A	L175 K178 L180	L165 K168 L170
BS02	A6M	A	V81 F90 T203 Y217 H219 Y326 I328 Y345 N376 M377 L399 L421	V71 F80 T193 Y207 H209 Y316 I318 Y335 N366 M367 L389 L411	MOAD: Ki=1406nM
BS03	MYA	A	H12 F14 W15 Y80 V81 L169 C170 V171 R176 E177 R179 A181 T189 V192 Y202 T203 L208 Y404	H2 F4 W5 Y70 V71 L159 C160 V161 R166 E167 R169 A171 T179 V182 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

External links

• PDB: RCSB:4cyn, PDBe:4cyn, PDBj:4cyn
• PDBsum: 4cyn
• PubMed: 25238611
• UniProt: Q4Q5S8