Structure of PDB 2qjo Chain C

Receptor sequence

>2qjoC (length=327) Species: 1148 (Synechocystis sp. PCC 6803)

KYQYGIYIGRFQPFHLGHLRTLNLALEKAEQVIIILGSHRVAADTRNPWR
SPERMAMIEACLSPQILKRVHFLTVRDWLYSDNLWLAAVQQQVLKITGGS
NSVVVLGHRKDASSYYLNLFPQWDYLETGHYPDFSSTAIRGAYFEGKEGD
YLDKVPPAIADYLQTFQKSERYIALCDEYQFLQAYKQAWATAPYAPTFIT
TDAVVVQAGHVLMVRRQAKPGLGLIALPGGFIKQNETLVEGMLRELKEET
RLKVPLPVLRGSIVDSHVFDAPGRSLRGRTITHAYFIQLPGGELPAVKAW
WMSLADLYAQEEQIYEDHFQIIQHFVS

3D structure

• PDB: 2qjo Bifunctional NMN Adenylyltransferase/ADP-Ribose Pyrophosphatase: Structure and Function in Bacterial NAD Metabolism.
• Chain: C
• 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	C	Y188 F201 T203 D205 R219 G232 G233 F234 E248 R277 R280 E326 H328	Y185 F198 T200 D202 R216 G229 G230 F231 E245 R274 R277 E316 H318
BS02	NAD	C	Y10 I11 G12 R13 G40 S41 D80 W81 D85 W88 H111 Y119 Y134	Y7 I8 G9 R10 G37 S38 D77 W78 D82 W85 H108 Y116 Y131
BS03	POP	C	R13 K113 S138 S139 T140 R143	R10 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)