Structure of PDB 1f7l Chain A

Receptor sequence
>1f7lA (length=118) Species: 1423 (Bacillus subtilis) [Search protein sequence]
GIYGIGLDITELKRIASMAGRQKRFAERILTRSELDQYYELSEKRKNEFL
AGRFAAKEAFSKAFGTGIGRQLSFQDIEIRKDQNGKPYIICTKLSPAAVH
VSITHTKEYAAAQVVIER
3D structure
PDB1f7l Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K62 H105
Catalytic site (residue number reindexed from 1) K62 H105
Enzyme Commision number 2.7.8.7: holo-[acyl-carrier-protein] synthase.
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 A D8 E58 D8 E58
BS02 COA A R53 G85 K86 P87 T104 H105 R53 G85 K86 P87 T104 H105
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008897 holo-[acyl-carrier-protein] synthase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0019878 lysine biosynthetic process via aminoadipic acid
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1f7l, PDBe:1f7l, PDBj:1f7l
PDBsum1f7l
PubMed10997907
UniProtP96618|ACPS_BACSU Holo-[acyl-carrier-protein] synthase (Gene Name=acpS)

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