Structure of PDB 3cb8 Chain A

Receptor sequence
>3cb8A (length=244) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
VIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEVT
VEDLMKEVVTYRHFMNASGGGVTASGGEAILQAEFVRDWFRACKKEGIHT
CLDTNGFVRRYDPVIDELLEVTDLVMLDLKQMNDEIHQNLVGVSNHRTLE
FAKYLANKNVKVWIRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLPY
HELGKHKWVAMGEEYKLDGVKPPKKETMERVKGILEQYGHKVMF
3D structure
PDB3cb8 Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme.
ChainA
Resolution2.77 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.97.1.4: [formate-C-acetyltransferase]-activating enzyme.
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 peptide A V15 D16 F25 H37 N38 L204 K208 V14 D15 F24 H36 N37 L203 K207
BS02 SAM A Y35 H37 G77 G78 D104 T105 D129 K131 V168 Y201 H202 Y34 H36 G76 G77 D103 T104 D128 K130 V167 Y200 H201
BS03 SF4 A C29 M31 C33 C36 W42 G78 N106 K131 C28 M30 C32 C35 W41 G77 N105 K130
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0030955 potassium ion binding
GO:0043365 [formate-C-acetyltransferase]-activating enzyme activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006006 glucose metabolic process
GO:0006974 DNA damage response
GO:0051604 protein maturation
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:3cb8, PDBe:3cb8, PDBj:3cb8
PDBsum3cb8
PubMed18852451
UniProtP0A9N4|PFLA_ECOLI Pyruvate formate-lyase 1-activating enzyme (Gene Name=pflA)

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