Structure of PDB 2nv2 Chain R

Receptor sequence
>2nv2R (length=193) Species: 1423 (Bacillus subtilis) [Search protein sequence]
MLTIGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGEST
TMRRLIDTYQFMEPLREFAAQGKPMFGTCAGLIILAKEIAGSDNPHLGLL
NVVVERNSFGRQVDSFEADLTIKGLDEPFTGVFIRAPHILEAGENVEVLS
EHNGRIVAAKQGQFLGCSFNPELTEDHRVTQLFVEMVEEYKQK
3D structure
PDB2nv2 Structure of a bacterial pyridoxal 5'-phosphate synthase complex
ChainR
Resolution2.12 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.2: glutaminase.
4.3.3.6: pyridoxal 5'-phosphate synthase (glutamine hydrolyzing).
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 GLN R G46 G47 S49 C79 A80 I83 R106 I134 R135 G46 G47 S49 C79 A80 I83 R106 I134 R135
Gene Ontology
Molecular Function
GO:0004359 glutaminase activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0016829 lyase activity
GO:0036381 pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
GO:0042802 identical protein binding
Biological Process
GO:0006541 glutamine metabolic process
GO:0006543 glutamine catabolic process
GO:0008614 pyridoxine metabolic process
GO:0042819 vitamin B6 biosynthetic process
GO:0042823 pyridoxal phosphate biosynthetic process
Cellular Component
GO:0005829 cytosol
GO:1903600 glutaminase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2nv2, PDBe:2nv2, PDBj:2nv2
PDBsum2nv2
PubMed17159152
UniProtP37528|PDXT_BACSU Pyridoxal 5'-phosphate synthase subunit PdxT (Gene Name=pdxT)

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