Structure of PDB 2qjt Chain A Binding Site BS01

Receptor Information

>2qjt Chain A (length=340) Species: 263 (Francisella tularensis)

MYDISVFIGRFQPFHKGHLHNIIIALQNSKKVIINIGSCFNTPNIKNPFS
FEQRKQMIESDLQVAGIDLDTVVIEPLADYFYQEQKWQDELRKNVYKHAK
NNNSIAIVGSSSYYIRSFPEWDYIGVDNYKNFNATEFRQKFYNGIISKQY
MCSNDPKLGTYNFLTKFMDTQVYQDLVAENNYVIEYKRLWLKAPFKPNFV
TVDALVIVNDHILMVQRKAHPGKDLWALPGGFLECDETIAQAIIRELFEE
TNINLTHEQLAIAKRCEKVFDYPDRSVRGRTISHVGLFVFDQWPSLPEIN
AADDAKDVKWISLGSNIKNICDRMLEDHYQIITILLEECG

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 2qjt Chain A Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2qjt Bifunctional NMN Adenylyltransferase/ADP-Ribose Pyrophosphatase: Structure and Function in Bacterial NAD Metabolism.
• Resolution: 2.3 Å
• Binding residue (original residue number in PDB): G234 E254 D308
• Binding residue (residue number reindexed from 1): G230 E250 D304
• Annotation score: 1

Enzymatic activity

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

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0000309 nicotinamide-nucleotide adenylyltransferase activity
• GO:0003824 catalytic activity
• GO:0016779 nucleotidyltransferase activity
• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0009058 biosynthetic process

External links

• PDB: RCSB:2qjt, PDBe:2qjt, PDBj:2qjt
• PDBsum: 2qjt
• PubMed: 18275811
• UniProt: Q5NHR1