Structure of PDB 2pza Chain A

Receptor sequence

>2pzaA (length=279) Species: 1392 (Bacillus anthracis)

MTLQEQIMKALHVQPVIDPKAEIRKRVDFLKDYVKKTGAKGFVLGISGGQ
DSTLAGRLAQLAVEEIRNEGGNATFIAVRLPYKVQKDEDDAQLALQFIQA
DQSVAFDIASTVDAFSNQYENLLDESLTDFNKGNVKARIRMVTQYAIGGQ
KGLLVIGTDHAAEAVTGFFTKFGDGGADLLPLTGLTKRQGRALLQELGAD
ERLYLKMPTADLLDEKPGQADETELGITYDQLDDYLEGKTVPADVAEKIE
KRYTVSEHKRQVPASMFDDWWKLAAALEH

3D structure

• PDB: 2pza Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD(+) synthetase from Bacillus anthracis.
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D51 E163
• Catalytic site (residue number reindexed from 1): D51 E163
• Enzyme Commision number: 6.3.1.5: NAD(+) 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	MG	A	D51 E163	D51 E163
BS02	AMP	A	G45 I46 S47 S52 R79 L80 Q85 R140 T158 E163 D174 T209 A210	G45 I46 S47 S52 R79 L80 Q85 R140 T158 E163 D174 T209 A210
BS03	POP	A	S47 G49 D51 S52 K187 P208 T209	S47 G49 D51 S52 K187 P208 T209

Gene Ontology

Molecular Function

• GO:0003952 NAD+ synthase (glutamine-hydrolyzing) activity
• GO:0004359 glutaminase activity
• GO:0005524 ATP binding
• GO:0008795 NAD+ synthase activity
• GO:0016874 ligase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0009435 NAD biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2pza, PDBe:2pza, PDBj:2pza
• PDBsum: 2pza
• PubMed: 17642516
• UniProt: Q81RP3|NADE_BACAN NH(3)-dependent NAD(+) synthetase (Gene Name=nadE)