Structure of PDB 3am3 Chain B

Receptor sequence

>3am3B (length=287) Species: 5833 (Plasmodium falciparum) [Search protein sequence]

NEDICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNG
KFDNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYTI
EDVANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSL
ISLCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVL
AYHLGRNYNIRINTISAGPLKSRAATAINTFIDYMIEYSEKYAPLRQKLL
STDIGSVASFLLSRESRAITGQTIYVDNGLNIMFLPD

3D structure

PDB

3am3 Effect of substrate binding loop mutations on the structure, kinetics, and inhibition of enoyl acyl carrier protein reductase from plasmodium falciparum

Chain

Resolution

2.5 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	NAD	B	G104 G106 G110 Y111 W131 F167 D168 A169 S215 L216 A217 N218 L265 T266 Y267 K285 A312 P314 L315 S317 A319	G9 G11 G15 Y16 W36 F72 D73 A74 S120 L121 A122 N123 L170 T171 Y172 K190 A217 P219 L220 S222 A224
BS02	TCL	B	A217 N218 A219 V222 Y267 Y277 M281 A319 A320 I323	A122 N123 A124 V127 Y172 Y182 M186 A224 A225 I228	MOAD: Ki=28nM BindingDB: IC50=200nM

Gene Ontology

	Molecular Function
GO:0004318	enoyl-[acyl-carrier-protein] reductase (NADH) activity

	Biological Process
GO:0006633	fatty acid biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:3am3, PDBe:3am3, PDBj:3am3
PDBsum	3am3
PubMed	21280175
UniProt	Q9BJJ9

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