Structure of PDB 2op1 Chain B

Receptor sequence

>2op1B (length=280) Species: 5833 (Plasmodium falciparum) [Search protein sequence]

DICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNGKF
DNDMIKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYTIEDVANLI
HQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSLISLCKYF
VNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVLAYHLGRN
YNIRINTISAGPLKSRAATAINTFIDYAIEYSEKYAPLRQKLLSTDIGSV
ASFLLSRESRAITGQTIYVDNGLNIMFLPD

3D structure

PDB

2op1 X-ray structural analysis of Plasmodium falciparum enoyl acyl carrier protein reductase as a pathway toward the optimization of triclosan antimalarial efficacy

Chain

Resolution

2.6 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)	Y175 K183
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 D168 A169 S215 L216 A217 N218 L265 T266 Y267 K285 A312 G313 P314 L315 S317 A319	G7 G9 G13 Y14 W34 D66 A67 S113 L114 A115 N116 L163 T164 Y165 K183 A210 G211 P212 L213 S215 A217
BS02	8PC	B	A217 N218 A219 V222 Y267 Y277 M281 A319 I323	A115 N116 A117 V120 Y165 Y175 M179 A217 I221

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:2op1, PDBe:2op1, PDBj:2op1
PDBsum	2op1
PubMed	17567585
UniProt	Q9BH77

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