Structure of PDB 1kqp Chain A Binding Site BS01

Receptor Information

>1kqp Chain A (length=271) Species: 1423 (Bacillus subtilis)

SMQEKIMRELHVKPSIDPKQEIEDRVNFLKQYVKKTGAKGFVLGISGGQD
STLAGRLAQLAVESIREEGGDAQFIAVRLPHGTQQDEDDAQLALKFIKPD
KSWKFDIKSTVSAFSDQYQQETGDQLTDFNKGNVKARTRMIAQYAIGGQE
GLLVLGTDHAAEAVTGFFTKYGDGGADLLPLTGLTKRQGRTLLKELGAPE
RLYLKEPTADLLDEKPQQSDETELGISYDEIDDYLEGKEVSAKVSEALEK
RYSMTEHKRQVPASMFDDWWK

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: 1kqp Chain A Residue 5001

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1kqp NH3-dependent NAD+ synthetase from Bacillus subtilis at 1 A resolution.
• Resolution: 1.03 Å
• Binding residue (original residue number in PDB): D50 E162
• Binding residue (residue number reindexed from 1): D50 E162
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): D50 E162
• Catalytic site (residue number reindexed from 1): D50 E162
• 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
• GO:0030435 sporulation resulting in formation of a cellular spore

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1kqp, PDBe:1kqp, PDBj:1kqp
• PDBsum: 1kqp
• PubMed: 12077433
• UniProt: P08164|NADE_BACSU NH(3)-dependent NAD(+) synthetase (Gene Name=nadE)