Structure of PDB 5eks Chain B

Receptor sequence

>5eksB (length=354) Species: 470 (Acinetobacter baumannii)

HHMQTLHVELRRYPIFIGSQLDPKQLLEPYIHGQQVMIVSNVTVAPLYLS
HYQEALESLGKTVATCILPDGEKYKDIQHLNLIFDALLEAGFNRDCTVLA
LGGGVIGDMAGFASACFQRGVYFVQVPTTLLSQVDSSVGGKTGINHPLGK
NMLGAFQQPQVVLADMAQLNTLPERELSAGLAEVIKYALLGDEDFLVWLE
ENMDGLVARDADLLAEAVYRSCAHKARIVANDEERALLNLGHTFGHAIES
YLGYGTWLHGEAVATGMVMAADLSQRLGWISNEDVARTKKIIQRANLPIS
CPQIPLDDFLGYMAHDKKVGQLRLVLLKQLGQAVITKDFDVELMKQAILA
NQHG

3D structure

• PDB: 5eks Structure of 3-dehydroquinate synthase from Acinetobacter baumannii in complex with NAD
• Chain: B
• Resolution: 1.85 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R119 K141 E183 K225 R239 N243 H246 H250 H263
• Catalytic site (residue number reindexed from 1): R119 K141 E183 K225 R235 N239 H242 H246 H259
• Enzyme Commision number: 4.2.3.4: 3-dehydroquinate 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	NAD	B	V44 D70 E72 K75 G103 G104 V105 D108 T128 T129 D135 K141 T171 L172 E176	V44 D70 E72 K75 G103 G104 V105 D108 T128 T129 D135 K141 T171 L172 E176
BS02	MG	B	E183 H246 H263	E183 H242 H259

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0003856 3-dehydroquinate synthase activity
• GO:0016829 lyase activity
• GO:0016838 carbon-oxygen lyase activity, acting on phosphates
• GO:0046872 metal ion binding

Biological Process

• GO:0008652 amino acid biosynthetic process
• GO:0009073 aromatic amino acid family biosynthetic process
• GO:0009423 chorismate biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:5eks, PDBe:5eks, PDBj:5eks
• PDBsum: 5eks
• UniProt: V5V8R5