Structure of PDB 2qjt Chain B

Receptor sequence
>2qjtB (length=344) Species: 263 (Francisella tularensis) [Search protein sequence]
MYDISVFIGRFQPFHKGHLHNIIIALQNSKKVIINIGSCFNTPNIKNPFS
FEQRKQMIESDLQVAGIDLDTVVIEPLADYFYQEQKWQDELRKNVYKHAK
NNNSIAIVGHIKDSSSYYIRSFPEWDYIGVDNYKNFNATEFRQKFYNGII
SKQYMCSNDPKLGTYNFLTKFMDTQVYQDLVAENNYVIEYKRLWLKAPFK
PNFVTVDALVIVNDHILMVQRKAHPGKDLWALPGGFLECDETIAQAIIRE
LFEETNINLTHEQLAIAKRCEKVFDYPDRSVRGRTISHVGLFVFDQWPSL
PEINAADDAKDVKWISLGSNIKNICDRMLEDHYQIITILLEECG
3D structure
PDB2qjt Bifunctional NMN Adenylyltransferase/ADP-Ribose Pyrophosphatase: Structure and Function in Bacterial NAD Metabolism.
ChainB
Resolution2.3 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 MN B E250 E254 D307 D308 E250 E254 D307 D308
BS02 MN B G234 E254 D308 G234 E254 D308
BS03 AMP B Y190 F203 G235 F236 E250 D308 Y190 F203 G235 F236 E250 D308
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2qjt, PDBe:2qjt, PDBj:2qjt
PDBsum2qjt
PubMed18275811
UniProtQ5NHR1

[Back to BioLiP]