Structure of PDB 1v35 Chain B

Receptor sequence
>1v35B (length=287) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
NEDICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNG
KFDNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYTI
EDVANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSL
ISLCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVL
AYHLGRNYNIRINTISAGPLKSRAATAINTFIDYAIEYSEKYAPLRQKLL
STDIGSVASFLLSRESRAITGQTIYVDNGLNIMFLPD
3D structure
PDB1v35 Structural basis for the variation in triclosan affinity to enoyl reductases.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y277 K285
Catalytic site (residue number reindexed from 1) Y182 K190
Enzyme Commision number 1.3.1.9: enoyl-[acyl-carrier-protein] reductase (NADH).
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 NAI B G104 I105 G106 G110 Y111 W131 D168 A169 S215 L216 A217 N218 L265 T266 Y267 K285 L315 S317 A319 G9 I10 G11 G15 Y16 W36 D73 A74 S120 L121 A122 N123 L170 T171 Y172 K190 L220 S222 A224 MOAD: Ki=96pM
Gene Ontology
Molecular Function
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
Biological Process
GO:0006633 fatty acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1v35, PDBe:1v35, PDBj:1v35
PDBsum1v35
PubMed15381426
UniProtQ9BJJ9

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