Structure of PDB 3uny Chain E

Receptor sequence

>3unyE (length=391) Species: 1396 (Bacillus cereus)

NKYKRIFLVVMDSVGIGEAPDAEQFGDLGSDTIGHIAEHMNGLQMPNMVK
LGLGNIREMKGISKVEKPLGYYTKMQEKSTGKDEMTGHWEIMGLYIDTPF
QVFPEGFPKELLDELEEKTGRKIIGNKPASGTEILDELGQEQMETGSLIV
YTSADSVLQIAAHEEVVPLDELYKICKIARELTLDEKYMVGRVIARPFVG
EPGNFTRTPNRHDYALKPFGRTVMNELKDSDYDVIAIGKISDIYDGEGVT
ESLRTKSNMDGMDKLVDTLNMDFTGLSFLNLVDFDALFGHRRDPQGYGEA
LQEYDARLPEVFAKLKEDDLLLITADHGNDPIHPGTDHTREYVPLLAYSP
SMKEGGQELPLRQTFADIGATVAENFGVKMPEYGTSFLNEL

3D structure

• PDB: 3uny Molecular Differences between a Mutase and a Phosphatase: Investigations of the Activation Step in Bacillus cereus Phosphopentomutase.
• Chain: E
• Resolution: 1.95 Å

Enzymatic activity

• Enzyme Commision number: 5.4.2.7: phosphopentomutase.

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	MN	E	E85 D156 D286 H291 H339	E84 D155 D285 H290 H338
BS02	MN	E	D13 E85 D327 H328	D12 E84 D326 H327
BS03	MN	E	G27 D28 H334	G26 D27 H333

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0008973 phosphopentomutase activity
• GO:0016853 isomerase activity
• GO:0030145 manganese ion binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006015 5-phosphoribose 1-diphosphate biosynthetic process
• GO:0006018 2-deoxyribose 1-phosphate catabolic process
• GO:0009117 nucleotide metabolic process
• GO:0043094 cellular metabolic compound salvage

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:3uny, PDBe:3uny, PDBj:3uny
• PDBsum: 3uny
• PubMed: 22329805
• UniProt: Q818Z9|DEOB_BACCR Phosphopentomutase (Gene Name=deoB)