Structure of PDB 4njj Chain A

Receptor sequence
>4njjA (length=209) Species: 395019 (Burkholderia multivorans ATCC 17616) [Search protein sequence]
TYAVKEIFYTLQGEGANAGRPAVFCRFAGCNLWSGREEDRAQAVCRFCDT
DFVGTDGENGGKFKDADALVATIAGLWPAGEAHRFVVCTGGEPMLQLDQP
LVDALHAAGFGIAIETNGSLPVLESIDWICVSPKADAPLVVTKGNELKVV
IPQDNQRLADYAKLDFEYFLVQPMDGPSRDLNTKLAIDWCKRHPQWRLSM
QTHKYLNIP
3D structure
PDB4njj Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F25 C31 C46 C49 D50 T51 E116 H204
Catalytic site (residue number reindexed from 1) F24 C30 C45 C48 D49 T50 E115 H203
Enzyme Commision number 4.3.99.3: 7-carboxy-7-deazaguanine 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 SF4 A C31 W34 C46 C49 F53 G92 N118 K135 C30 W33 C45 C48 F52 G91 N117 K134
BS02 SAM A F48 D50 G92 E116 T117 N118 S133 K135 V151 Q173 M175 D176 Q202 F47 D49 G91 E115 T116 N117 S132 K134 V150 Q172 M174 D175 Q201
BS03 2K8 A E15 F25 R27 T90 H204 P210 E14 F24 R26 T89 H203 P209
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0016840 carbon-nitrogen lyase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
GO:1904047 S-adenosyl-L-methionine binding
Biological Process
GO:0008616 queuosine biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4njj, PDBe:4njj, PDBj:4njj
PDBsum4njj
PubMed24362703
UniProtA0A0H3KB22|QUEE_BURM1 7-carboxy-7-deazaguanine synthase (Gene Name=queE)

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