Structure of PDB 4dlk Chain B Binding Site BS01

Receptor Information

>4dlk Chain B (length=380) Species: 592021 (Bacillus anthracis str. A0248)

MTRIILPGKTIGIIGGGQLGRMMALAAKEMGYKIAVLDPTKNSPCAQVAD
IEIVASYDDLKAIQHLAEISDVVTYEFENIDYRCLQWLEKHAYLPQGSQL
LSKTQNRFTEKNAIEKAGLPVATYRLVQNQEQLTEAIAELSYPSVLKTTT
GGYDGKGQVVLRSEADVDEARKLANAAECILEKWVPFEKEVSVIVIRSVS
GETKVFPVAENIHVNNILHESIVPARITEELSQKAIAYAKVLADELELVG
TLAVEMFATADGEIYINELAPRPHNSGHYTQDACETSQFGQHIRAICNLP
LGETNLLKPVVMVNILGEHIEGVLRQVNRLTGCYLHLYGKEEAKAQRKMG
HVNILNDNIEVALEKAKSLHIWDHQEQLLE

Ligand information

• Ligand ID: CA
• InChI: InChI=1S/Ca/q+2
• InChIKey: BHPQYMZQTOCNFJ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Ca++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Ca+2]
• Formula: Ca
• Name: CALCIUM ION
• DrugBank: DB14577
• PDB chain: 4dlk Chain B Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4dlk Elucidation of the bicarbonate binding site and insights into the carboxylation mechanism of (N(5))-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis.
• Resolution: 2.02 Å
• Binding residue (original residue number in PDB): E255 E268
• Binding residue (residue number reindexed from 1): E255 E268
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): Y153 G155 E255 E268 N275 S276 K348
• Catalytic site (residue number reindexed from 1): Y153 G155 E255 E268 N275 S276 K348
• Enzyme Commision number: 6.3.4.18: 5-(carboxyamino)imidazole ribonucleotide synthase.

Gene Ontology

Molecular Function

• GO:0004638 phosphoribosylaminoimidazole carboxylase activity
• GO:0005524 ATP binding
• GO:0016829 lyase activity
• GO:0016874 ligase activity
• GO:0034028 5-(carboxyamino)imidazole ribonucleotide synthase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006164 purine nucleotide biosynthetic process
• GO:0006189 'de novo' IMP biosynthetic process

External links

• PDB: RCSB:4dlk, PDBe:4dlk, PDBj:4dlk
• PDBsum: 4dlk
• PubMed: 25372694
• UniProt: A0A6L8P0X7