Structure of PDB 2wuu Chain A

Receptor sequence
>2wuuA (length=402) Species: 5661 (Leishmania donovani) [Search protein sequence]
AHAFWSTQPVPQTEDETEKIVFAGPMDEPKTVADIPEEPYPIASTFEWWT
PNMEAADDIHAIYELLRDNYVESMFRFNYSEEFLQWALCPPSYIPDWHVA
VRRKADKKLLAFIAGVPVTLRMGTPKYMKVKAQEKGQEEEAAKYDAPRHI
CEINFLCVHKQLREKRLAPILIKEVTRRVNRTNVWQAVYTAGVLLPTPYA
SGQYFHRSLNPEKLVEIRFSGIPAQYQKFQNPMAMLKRNYQLPNAPKNSG
LREMKPSDVPQVRRILMNYLDNFDVGPVFSDAEISHYLLPRDGVVFTYVV
ENDKKVTDFFSFYRIPSTVIILNAAYVHYYAATSMPLHQLILDLLIVAHS
RGFDVCNMVEILDNRSFVEQLKFGAGDGHLRYYFYNWAYPKIKPSQVALV
ML
3D structure
PDB2wuu N-Myristoyltransferase from Leishmania Donovani: Structural and Functional Characterisation of a Potential Drug Target for Visceral Leishmaniasis.
ChainA
Resolution1.42 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) N154 F155 L156 T190 L402
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 NHW A H12 A13 F14 W15 Y80 V81 I166 N167 L169 C170 V171 R176 E177 R179 L180 A181 P182 I185 T189 V192 W198 A200 Y202 T203 A204 L208 Y404 H2 A3 F4 W5 Y70 V71 I153 N154 L156 C157 V158 R163 E164 R166 L167 A168 P169 I172 T176 V179 W185 A187 Y189 T190 A191 L195 Y385 MOAD: ic50=68.7nM
PDBbind-CN: -logKd/Ki=7.16,IC50=68.7nM
Gene Ontology
Molecular Function
GO:0004379 glycylpeptide N-tetradecanoyltransferase activity
GO:0016746 acyltransferase activity
Biological Process
GO:0006499 N-terminal protein myristoylation
GO:0018008 N-terminal peptidyl-glycine N-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:2wuu, PDBe:2wuu, PDBj:2wuu
PDBsum2wuu
PubMed20036251
UniProtD0AB09

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