Structure of PDB 4cyq Chain A

Receptor sequence

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

AHAFWSTQPVPQTEDETEKIVFAGPMDEPKTVADIPEEPYPIASTFEWWT
PNMEAADDIHAIYELLRDNYVEDDDSMFRFNYSEEFLQWALCPPNYIPDW
HVAVRRKADKKLLAFIAGVPVTLRMGTPKYMKVKAQEKGEGEEAAKYDEP
RHICEINFLCVHKQLREKRLAPILIKEATRRVNRTNVWQAVYTAGVLLPT
PYASGQYFHRSLNPEKLVEIRFSGIPAQYQKFQNPMAMLKRNYQLPSAPK
NSGLREMKPSDVPQVRRILMNYLDSFDVGPVFSDAEISHYLLPRDGVVFT
YVVENDKKVTDFFSFYRIPSTVIGNSNYNLLNAAYVHYYAATSIPLHQLI
LDLLIVAHSRGFDVCNMVEILDNRSFVEQLKFGAGDGHLRYYFYNWAYPK
IKPSQVALVML

3D structure

• PDB: 4cyq Structure-Based Design of Potent and Selective Leishmania N- Myristoyltransferase Inhibitors.
• Chain: A
• Resolution: 1.65 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 E177 K178 L180	L165 E167 K168 L170
BS02	YAU	A	V81 D83 F88 R89 F90 N167 T203 Y217 Y326 I328 Y345 N376 L399 M420 L421	V71 D73 F78 R79 F80 N157 T193 Y207 Y316 I318 Y335 N366 L389 M410 L411	MOAD: Ki=59nM
BS03	MYA	A	H12 F14 W15 Y80 V81 I166 L169 C170 V171 R176 E177 R179 A181 P182 T189 V192 Q199 A200 Y202 T203 L208 Y404	H2 F4 W5 Y70 V71 I156 L159 C160 V161 R166 E167 R169 A171 P172 T179 V182 Q189 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

External links

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