Structure of PDB 1n1d Chain B

Receptor sequence
>1n1dB (length=126) Species: 1423 (Bacillus subtilis) [Search protein sequence]
MKKVITYGTFDLLHWGHIKLLERAKQLGDYLVVAISTDEFNLQKQKKAYH
SYEHRKLILETIRYVDEVIPEKNWEQKKQDIIDHNIDVFVMGDDWEGKFD
FLKDQCEVVYLPRTEGISTTKIKEEI
3D structure
PDB1n1d Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K44 K46
Catalytic site (residue number reindexed from 1) K44 K46
Enzyme Commision number 2.7.7.39: glycerol-3-phosphate cytidylyltransferase.
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 SO4 B H14 H17 S118 T119 H14 H17 S118 T119
BS02 C2G B G8 T9 F10 K44 E71 G92 W95 F99 R113 T114 I117 G8 T9 F10 K44 E71 G92 W95 F99 R113 T114 I117
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
GO:0047348 glycerol-3-phosphate cytidylyltransferase activity
Biological Process
GO:0009058 biosynthetic process
GO:0019350 teichoic acid biosynthetic process
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1n1d, PDBe:1n1d, PDBj:1n1d
PDBsum1n1d
PubMed14506262
UniProtP27623|TAGD_BACSU Glycerol-3-phosphate cytidylyltransferase (Gene Name=tagD)

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