Structure of PDB 1n1d Chain B Binding Site BS01

Receptor Information

>1n1d Chain B (length=126) Species: 1423 (Bacillus subtilis)

MKKVITYGTFDLLHWGHIKLLERAKQLGDYLVVAISTDEFNLQKQKKAYH
SYEHRKLILETIRYVDEVIPEKNWEQKKQDIIDHNIDVFVMGDDWEGKFD
FLKDQCEVVYLPRTEGISTTKIKEEI

Ligand information

• Ligand ID: SO4
• InChI: InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
• InChIKey: QAOWNCQODCNURD-UHFFFAOYSA-L
• SMILES:
  OpenEye OEToolkits 1.5.0: [O-]S(=O)(=O)[O-]
  CACTVS 3.341: [O-][S]([O-])(=O)=O
  ACDLabs 10.04: [O-]S([O-])(=O)=O
• Formula: O4 S
• Name: SULFATE ION
• DrugBank: DB14546
• PDB chain: 1n1d Chain B Residue 705

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1n1d Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): H14 H17 S118 T119
• Binding residue (residue number reindexed from 1): H14 H17 S118 T119
• Annotation score: 1

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.

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

External links

• PDB: RCSB:1n1d, PDBe:1n1d, PDBj:1n1d
• PDBsum: 1n1d
• PubMed: 14506262
• UniProt: P27623|TAGD_BACSU Glycerol-3-phosphate cytidylyltransferase (Gene Name=tagD)