Structure of PDB 4mrt Chain A

Receptor sequence
>4mrtA (length=225) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
MKIYGIYMDRPLSQEENERFMTFISPEKREKCRRFYHKEDAHRTLLGDVL
VRSVISRQYQLDKSDIRFSTQEYGKPCIPDLPDAHFNISHSGRWVIGAFD
SQPIGIDIEKTKPISLEIAKRFFSKTEYSDLLAKDKDEQTDYFYHLWSMK
ESFIKQEGKGLSLPLDSFSVRLHQDGQVSIELPDSHSPCYIKTYEVDPGY
KMAVCAAHPDFPEDITMVSYEELLR
3D structure
PDB4mrt Crystal Structure of a PCP/Sfp Complex Reveals the Structural Basis for Carrier Protein Posttranslational Modification.
ChainA
Resolution2.0 Å
3D
structure
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Enzymatic activity
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 MG A D107 E151 D107 E151
BS02 COA A T44 Y73 G74 K75 P76 N87 I88 S89 H90 E151 K155 G160 L161 S162 T44 Y73 G74 K75 P76 N87 I88 S89 H90 E151 K155 G160 L161 S162
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:0017000 antibiotic biosynthetic process
GO:0019878 lysine biosynthetic process via aminoadipic acid
GO:1900192 positive regulation of single-species biofilm formation
Cellular Component
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:4mrt, PDBe:4mrt, PDBj:4mrt
PDBsum4mrt
PubMed24704508
UniProtP39135|SFP_BACSU 4'-phosphopantetheinyl transferase Sfp (Gene Name=sfp)

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