Structure of PDB 4nr0 Chain A

Receptor sequence
>4nr0A (length=259) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
GFLTGKRALIVGVASKLSIASGIAAAMHREGAELAFTYQNDKLRGRVEEF
ASGWGSRPELCFPCDVADDSQIEAVFAALGKHWDGLDIIVHSVGFAPGDQ
LDGDFTAVTTREGFRIAHDISAYSFIALAKAGREMMKGRNGSLLTLSYLG
AERTMPNYNVMGMAKASLEAGVRYLAGSLGAEGTRVNAVSAGPIRTLAAS
GIKSFRKMLAANERQTPLRRNVTIEEVGNAGAFLCSDLASGISGEILYVD
GGFNTTAMG
3D structure
PDB4nr0 Crystal Structures of Pseudomonas aeruginosa Enoyl-ACP Reductase (FabI) in the Presence and Absence of NAD+ and Triclosan
ChainA
Resolution1.799 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y159 K166
Catalytic site (residue number reindexed from 1) Y158 K165
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 A G13 A15 S19 I20 Q40 D66 V67 S93 V94 G95 L147 S148 Y149 K166 A192 P194 I195 T197 A199 G12 A14 S18 I19 Q39 D65 V66 S92 V93 G94 L146 S147 Y148 K165 A191 P193 I194 T196 A198
BS02 TCL A G95 A97 L102 Y149 Y159 A199 A200 G94 A96 L101 Y148 Y158 A198 A199
Gene Ontology
Molecular Function
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0030497 fatty acid elongation

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Molecular Function
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Biological Process
External links
PDB RCSB:4nr0, PDBe:4nr0, PDBj:4nr0
PDBsum4nr0
PubMed
UniProtQ9ZFE4|FABI_PSEAE Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (Gene Name=fabI)

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