Structure of PDB 4cyq Chain A Binding Site BS01

Receptor Information

>4cyq Chain A (length=411) Species: 5664 (Leishmania major)

AHAFWSTQPVPQTEDETEKIVFAGPMDEPKTVADIPEEPYPIASTFEWWT
PNMEAADDIHAIYELLRDNYVEDDDSMFRFNYSEEFLQWALCPPNYIPDW
HVAVRRKADKKLLAFIAGVPVTLRMGTPKYMKVKAQEKGEGEEAAKYDEP
RHICEINFLCVHKQLREKRLAPILIKEATRRVNRTNVWQAVYTAGVLLPT
PYASGQYFHRSLNPEKLVEIRFSGIPAQYQKFQNPMAMLKRNYQLPSAPK
NSGLREMKPSDVPQVRRILMNYLDSFDVGPVFSDAEISHYLLPRDGVVFT
YVVENDKKVTDFFSFYRIPSTVIGNSNYNLLNAAYVHYYAATSIPLHQLI
LDLLIVAHSRGFDVCNMVEILDNRSFVEQLKFGAGDGHLRYYFYNWAYPK
IKPSQVALVML

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 4cyq Chain A Residue 999

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4cyq Structure-Based Design of Potent and Selective Leishmania N- Myristoyltransferase Inhibitors.
• Resolution: 1.65 Å
• Binding residue (original residue number in PDB): L175 E177 K178 L180
• Binding residue (residue number reindexed from 1): L165 E167 K168 L170
• Annotation score: 1

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.

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