Structure of PDB 1ee1 Chain B

Receptor sequence
>1ee1B (length=246) Species: 1423 (Bacillus subtilis) [Search protein sequence]
SMQEKIMRELHVKPSIDPKQEIEDRVNFLKQYVKKTGAKGFVLGISGGQD
STLAGRLAQLAVESIREEGGDAQFIAVRLPHGEDDAQLALKFIKPDKSWK
FDIKSTVSAFSDQYQQETGDQLTDFNKGNVKARTRMIAQYAIGGQEGLLV
LGTDHAAEAVTGFFTKYGDGGADLLPLTGLTKRQGRTLLKELGAPERLYL
ISYDEIDDYLEGKEVSAKVSEALEKRYSMTEHKRQVPASMFDDWWK
3D structure
PDB1ee1 Stabilization of active-site loops in NH3-dependent NAD+ synthetase from Bacillus subtilis.
ChainB
Resolution2.06 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) D50 E162
Catalytic site (residue number reindexed from 1) D50 E158
Enzyme Commision number 6.3.1.5: NAD(+) synthase.
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 B Y32 Y144 L153 D177 Y32 Y140 L149 D173
BS02 DND B F129 N133 F167 F168 T169 K170 D173 H257 K258 F125 N129 F163 F164 T165 K166 D169 H232 K233
Gene Ontology
Molecular Function
GO:0003952 NAD+ synthase (glutamine-hydrolyzing) activity
GO:0004359 glutaminase activity
GO:0005524 ATP binding
GO:0008795 NAD+ synthase activity
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0009435 NAD biosynthetic process
GO:0030435 sporulation resulting in formation of a cellular spore
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1ee1, PDBe:1ee1, PDBj:1ee1
PDBsum1ee1
PubMed11375500
UniProtP08164|NADE_BACSU NH(3)-dependent NAD(+) synthetase (Gene Name=nadE)

[Back to BioLiP]