Structure of PDB 3tqv Chain B

Receptor sequence
>3tqvB (length=280) Species: 177416 (Francisella tularensis subsp. tularensis SCHU S4) [Search protein sequence]
NTDQINKVPNDIVTRLVRESLAEDIATGDITAQLAEDIDTTAFCITREEM
ILCGQDFANEVINQLDKNIQITWLYSDAQKVPANARIFELKGNVRSILTA
ERTILNFIQMLSGTATVTNKLVKLISQYKTKLLDTRKTIPGFRLAQKYAV
RCGGGFNHRIGLFDAYLIKENHIRSAGGIAKAVTKAKKLDSNKVVEVEVT
NLDELNQAIAAKADIVMLDNFSGEDIDIAVSIARGKVALEVSGNIDRNSI
VAIAKTGVDFISVGAITKHIKAIDLSLQVQ
3D structure
PDB3tqv Rapid countermeasure discovery against Francisella tularensis based on a metabolic network reconstruction.
ChainB
Resolution2.62 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R108 K143 K175 E204 D225
Catalytic site (residue number reindexed from 1) R102 K137 K169 E198 D219
Enzyme Commision number 2.4.2.19: nicotinate-nucleotide diphosphorylase (carboxylating).
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 PO4 B K143 N250 G270 K274 K137 N244 G264 K268
BS02 PO4 B T141 R142 H164 R165 L173 T135 R136 H158 R159 L167
Gene Ontology
Molecular Function
GO:0004514 nicotinate-nucleotide diphosphorylase (carboxylating) activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
Biological Process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process
GO:0034213 quinolinate catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3tqv, PDBe:3tqv, PDBj:3tqv
PDBsum3tqv
PubMed23704901
UniProtQ5NEY8

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