Structure of PDB 5u7f Chain A Binding Site BS01

Receptor Information

>5u7f Chain A (length=144) Species: 83334 (Escherichia coli O157:H7)

VYKRPVSILVVIYAQDTKRVLMLQRRDDPDFWQSVTGSVEEGETAPQAAM
REVKEEVTIDVVAEQLTLIDCQRTVEFEIFSHLRHRYAPGVTRNTESWFC
LALPHERQIVFTEHLAYKWLDAPAAAALTKSWSNRQAIEQFVIN

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: 5u7f Chain A Residue 201

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5u7f Metal ion coordination in the E. coli Nudix hydrolase dihydroneopterin triphosphate pyrophosphatase: New clues into catalytic mechanism.
• Resolution: 1.789 Å
• Binding residue (original residue number in PDB): E82 R97 W136
• Binding residue (residue number reindexed from 1): E78 R93 W132
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.6.1.67: dihydroneopterin triphosphate diphosphatase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0008828 dATP diphosphatase activity
• GO:0016787 hydrolase activity
• GO:0019177 dihydroneopterin triphosphate pyrophosphohydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0046654 tetrahydrofolate biosynthetic process
• GO:0046656 folic acid biosynthetic process

External links

• PDB: RCSB:5u7f, PDBe:5u7f, PDBj:5u7f
• PDBsum: 5u7f
• PubMed: 28742822
• UniProt: P0AFC0|NUDB_ECOLI Dihydroneopterin triphosphate diphosphatase (Gene Name=nudB)