Structure of PDB 2qjo Chain B

Receptor sequence

>2qjoB (length=336) Species: 1148 (Synechocystis sp. PCC 6803)

KYQYGIYIGRFQPFHLGHLRTLNLALEKAEQVIIILGSHRVAADTRNPWR
SPERMAMIEACLSPQILKRVHFLTVRDWLYSDNLWLAAVQQQVLKITGGS
NSVVVLGHRKDASSYYLNLFPQWDYLETGHYPDFSSTAIRGAYFEGKEGD
YLDKVPPAIADYLQTFQKSERYIALCDEYQFLQAYKQAWATAPYAPTFIT
TDAVVVQAGHVLMVRRQAKPGLGLIALPGGFIKQNETLVEGMLRELKEET
RLKVPLPVLRGSIVDSHVFDAPGRSLRGRTITHAYFIQLPGGELPAVKGG
DDAQKAWWMSLADLYAQEEQIYEDHFQIIQHFVSKV

3D structure

• PDB: 2qjo Bifunctional NMN Adenylyltransferase/ADP-Ribose Pyrophosphatase: Structure and Function in Bacterial NAD Metabolism.
• Chain: B
• Resolution: 2.6 Å

Enzymatic activity

• Enzyme Commision number: 2.7.7.1: nicotinamide-nucleotide adenylyltransferase.
  3.6.1.-

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	APR	B	Y188 F201 T203 D205 R219 G232 G233 F234 E248 R277 R280 E326 H328	Y185 F198 T200 D202 R216 G229 G230 F231 E245 R274 R277 E323 H325
BS02	NAD	B	Y10 I11 G12 R13 H21 G40 S41 D80 W81 D85 W88 H111 K113 Y118 Y119 H133 Y134	Y7 I8 G9 R10 H18 G37 S38 D77 W78 D82 W85 H108 K110 Y115 Y116 H130 Y131
BS03	POP	B	R13 R49 K113 S138 S139 T140 R143	R10 R46 K110 S135 S136 T137 R140

Gene Ontology

Molecular Function

• GO:0000309 nicotinamide-nucleotide adenylyltransferase activity
• GO:0003824 catalytic activity
• GO:0005524 ATP binding
• GO:0016779 nucleotidyltransferase activity
• GO:0016787 hydrolase activity
• GO:0042802 identical protein binding

Biological Process

• GO:0009058 biosynthetic process
• GO:0009435 NAD biosynthetic process
• GO:0019363 pyridine nucleotide biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2qjo, PDBe:2qjo, PDBj:2qjo
• PDBsum: 2qjo
• PubMed: 18275811
• UniProt: Q55928|NADM_SYNY3 Bifunctional NMN adenylyltransferase/Nudix hydrolase (Gene Name=slr0787)