Structure of PDB 4njg Chain B

Receptor sequence

>4njgB (length=209) Species: 395019 (Burkholderia multivorans ATCC 17616)

TYAVKEIFYTLQGEGANAGRPAVFCRFAGCNLWSGREEDRAQAVCRFCDT
DFVGTDGENGGKFKDADALVATIAGLWPAGEAHRFVVCTGGEPMLQLDQP
LVDALHAAGFGIAIETNGSLPVLESIDWICVSPKADAPLVVTKGNELKVV
IPQDNQRLADYAKLDFEYFLVQPMDGPSRDLNTKLAIDWCKRHPQWRLSM
QTHKYLNIP

3D structure

• PDB: 4njg Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism.
• Chain: B
• Resolution: 2.598 Å

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	B	C31 W34 C46 C49 F53 G92 N118 K135	C30 W33 C45 C48 F52 G91 N117 K134
BS02	SAM	B	F48 D50 T51 G91 G92 E116 T117 N118 S133 K135 V151 Q173 M175 D176 Q202	F47 D49 T50 G90 G91 E115 T116 N117 S132 K134 V150 Q172 M174 D175 Q201
BS03	HHS	B	G14 F25 R27 T90 H204 P210	G13 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

External links

• PDB: RCSB:4njg, PDBe:4njg, PDBj:4njg
• PDBsum: 4njg
• PubMed: 24362703
• UniProt: A0A0H3KB22|QUEE_BURM1 7-carboxy-7-deazaguanine synthase (Gene Name=queE)