Structure of PDB 2qtr Chain A

Receptor sequence
>2qtrA (length=189) Species: 1392 (Bacillus anthracis) [Search protein sequence]
MRKIGIIGGTFDPPHYGHLLIANEVYHALNLEEVWFLPNQIPPHKQGRNI
TSVESRLQMLELATEAEEHFSICLEELSRKGPSYTYDTMLQLTKKYPDVQ
FHFIIGGDMVEYLPKWYNIEALLDLVTFVGVARPGYKLRTPYPITTVEIP
EFAVSSSLLRERYKEKKTCKYLLPEKVQVYIERNGLYES
3D structure
PDB2qtr Kinetic and X-ray structural evidence for negative cooperativity in substrate binding to nicotinate mononucleotide adenylyltransferase (NMAT) from Bacillus anthracis.
ChainA
Resolution1.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.18: nicotinate-nucleotide adenylyltransferase.
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 DND A G8 G9 T10 H18 P43 H44 Y84 T85 G106 D108 M109 W116 R133 F152 V154 G8 G9 T10 H18 P43 H44 Y84 T85 G106 D108 M109 W116 R133 F152 V154 MOAD: Kd=3.2uM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004515 nicotinate-nucleotide adenylyltransferase activity
GO:0005524 ATP binding
GO:0016779 nucleotidyltransferase activity
GO:0070566 adenylyltransferase activity
Biological Process
GO:0009058 biosynthetic process
GO:0009165 nucleotide biosynthetic process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2qtr, PDBe:2qtr, PDBj:2qtr
PDBsum2qtr
PubMed18977360
UniProtC3L5T6|NADD_BACAC Probable nicotinate-nucleotide adenylyltransferase (Gene Name=nadD)

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