Structure of PDB 5eks Chain A

Receptor sequence

>5eksA (length=355) Species: 470 (Acinetobacter baumannii)

HMQTLHVELGERRYPIFIGSQLDPKQLLEPYIHGQQVMIVSNVTVAPLYL
SHYQEALESLGKTVATCILPDGEKYKDIQHLNLIFDALLEAGFNRDCTVL
ALGGGVIGDMAGFASACFQRGVYFVQVPTTLLSQVDSSVGGKTGINHPLG
KNMLGAFQQPQVVLADMAQLNTLPERELSAGLAEVIKYALLGDEDFLVWL
EENMDGLVARDADLLAEAVYRSCAHKARIVANDEKERALLNLGHTFGHAI
ESYLGYGTWLHGEAVATGMVMAADLSQRLGWISNEDVARTKKIIQRANLP
ISCPQIPLDDFLGYMAHDKKVQLRLVLLKQLGQAVITKDFDVELMKQAIL
ANQHG

3D structure

• PDB: 5eks Structure of 3-dehydroquinate synthase from Acinetobacter baumannii in complex with NAD
• Chain: A
• 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): R120 K142 E184 K226 R237 N241 H244 H248 H261
• 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	A	N41 V44 D70 E72 K75 G103 G104 V105 D108 T128 T129 D135 S136 K141 T171 L172 E176	N42 V45 D71 E73 K76 G104 G105 V106 D109 T129 T130 D136 S137 K142 T172 L173 E177
BS02	MG	A	E183 H246 H263	E184 H244 H261

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