Structure of PDB 1q7c Chain B

Receptor sequence
>1q7cB (length=243) Species: 562 (Escherichia coli) [Search protein sequence]
NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGA
NGKGLMLNVTDPASIESVLEKIRAEFGEVDILVNNAGITRDNLLMRMKDE
EWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANF
AAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGIL
AQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMYMV
3D structure
PDB1q7c Cofactor-Induced Conformational Rearrangements Establish a Catalytically Competent Active Site and a Proton Relay Conduit in FabG
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) G16 S138 Q148 F151 K155
Catalytic site (residue number reindexed from 1) G15 S137 Q147 F150 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 NDP B S14 A36 T37 L58 N59 V60 G88 I89 S13 A35 T36 L57 N58 V59 G87 I88
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:1q7c, PDBe:1q7c, PDBj:1q7c
PDBsum1q7c
PubMed15016358
UniProtP0AEK2|FABG_ECOLI 3-oxoacyl-[acyl-carrier-protein] reductase FabG (Gene Name=fabG)

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