Structure of PDB 1q7b Chain D

Receptor sequence
>1q7bD (length=243) Species: 562 (Escherichia coli) [Search protein sequence]
NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGA
NGKGLMLNVTDPASIESVLEKIRAEFGEVDILVNNAGITRDNLLMRMKDE
EWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANY
AAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGIL
AQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMYMV
3D structure
PDB1q7b Cofactor-Induced Conformational Rearrangements Establish a Catalytically Competent Active Site and a Proton Relay Conduit in FabG
ChainD
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G16 E102 S138 Q148 Y151 K155
Catalytic site (residue number reindexed from 1) G15 E101 S137 Q147 Y150 K154
Enzyme Commision number 1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase.
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 CA D E233 T234 E232 T233
BS02 NAP D G12 S14 R15 T37 N59 V60 N86 A87 S138 Y151 K155 P181 I184 G11 S13 R14 T36 N58 V59 N85 A86 S137 Y150 K154 P180 I183 MOAD: Kd=3.5uM
Gene Ontology
Molecular Function
GO:0004316 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0050661 NADP binding
GO:0051287 NAD binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0008610 lipid biosynthetic process
GO:0009102 biotin biosynthetic process
GO:0030497 fatty acid elongation
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1q7b, PDBe:1q7b, PDBj:1q7b
PDBsum1q7b
PubMed15016358
UniProtP0AEK2|FABG_ECOLI 3-oxoacyl-[acyl-carrier-protein] reductase FabG (Gene Name=fabG)

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