Structure of PDB 2pza Chain A Binding Site BS01

Receptor Information

>2pza Chain A (length=279) Species: 1392 (Bacillus anthracis)

MTLQEQIMKALHVQPVIDPKAEIRKRVDFLKDYVKKTGAKGFVLGISGGQ
DSTLAGRLAQLAVEEIRNEGGNATFIAVRLPYKVQKDEDDAQLALQFIQA
DQSVAFDIASTVDAFSNQYENLLDESLTDFNKGNVKARIRMVTQYAIGGQ
KGLLVIGTDHAAEAVTGFFTKFGDGGADLLPLTGLTKRQGRALLQELGAD
ERLYLKMPTADLLDEKPGQADETELGITYDQLDDYLEGKTVPADVAEKIE
KRYTVSEHKRQVPASMFDDWWKLAAALEH

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 2pza Chain A Residue 6242

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2pza Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD(+) synthetase from Bacillus anthracis.
• Resolution: 2.4 Å
• Binding residue (original residue number in PDB): D51 E163
• Binding residue (residue number reindexed from 1): D51 E163
• Annotation score: 1

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.

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)