Structure of PDB 4dlk Chain B

Receptor sequence

>4dlkB (length=380) Species: 592021 (Bacillus anthracis str. A0248)

MTRIILPGKTIGIIGGGQLGRMMALAAKEMGYKIAVLDPTKNSPCAQVAD
IEIVASYDDLKAIQHLAEISDVVTYEFENIDYRCLQWLEKHAYLPQGSQL
LSKTQNRFTEKNAIEKAGLPVATYRLVQNQEQLTEAIAELSYPSVLKTTT
GGYDGKGQVVLRSEADVDEARKLANAAECILEKWVPFEKEVSVIVIRSVS
GETKVFPVAENIHVNNILHESIVPARITEELSQKAIAYAKVLADELELVG
TLAVEMFATADGEIYINELAPRPHNSGHYTQDACETSQFGQHIRAICNLP
LGETNLLKPVVMVNILGEHIEGVLRQVNRLTGCYLHLYGKEEAKAQRKMG
HVNILNDNIEVALEKAKSLHIWDHQEQLLE

3D structure

• PDB: 4dlk Elucidation of the bicarbonate binding site and insights into the carboxylation mechanism of (N(5))-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis.
• Chain: B
• Resolution: 2.02 Å

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.

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	CA	B	E255 E268	E255 E268
BS02	CA	B	G152 E268	G152 E268
BS03	ATP	B	R107 K147 Y153 D154 G155 Q158 E182 W184 V185 F187 E190 H213 N216 E255 F257 E268	R107 K147 Y153 D154 G155 Q158 E182 W184 V185 F187 E190 H213 N216 E255 F257 E268

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