Structure of PDB 1nvb Chain B

Receptor sequence

>1nvbB (length=391) Species: 162425 (Aspergillus nidulans)

NPTKISILGRESIIADFGLWRNYVAKDLISDCSSTTYVLVTDTNIGSIYT
PSFEEAFRKRAAEITPSPRLLIYNRPPGEVSKSRQTKADIEDWMLSQNPP
CGRDTVVIALGGGVIGDLTGFVASTYMRGVRYVQVPTTLLAMVDSSIGGK
TAIDTPLGKNLIGAIWQPTKIYIDLEFLETLPVREFINGMAEVIKTAAIS
SEEEFTALEENAETILKAVRREVTPGEHRFEGTEEILKARILASARHKAY
VVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELA
RHLGILKGVAVSRIVKCLAAYGLPTSLKDARIRKLTAGKHCSVDQLMFNM
ALDKKNDGPKKKIVLLSAIGTPYETRASVVANEDIRVVLAP

3D structure

• PDB: 1nvb Ligand-induced Conformational Changes and a Mechanism for Domain Closure in Aspergillus nidulans Dehydroquinate Synthase
• Chain: B
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R130 K152 E194 K250 E260 R264 N268 H271 H275 H287
• Catalytic site (residue number reindexed from 1): R128 K150 E192 K248 E258 R262 N266 H269 H273 H285
• Enzyme Commision number: 1.1.1.25: shikimate dehydrogenase (NADP(+)).
  2.5.1.19: 3-phosphoshikimate 1-carboxyvinyltransferase.
  2.7.1.71: shikimate kinase.
  4.2.1.10: 3-dehydroquinate dehydratase.
  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	ZN	B	E194 H271 H287	E192 H269 H285
BS02	CRB	B	D146 K152 N162 E194 K250 R264 L267 N268 H271 H275 K356	D144 K150 N160 E192 K248 R262 L265 N266 H269 H273 K354

Gene Ontology

Molecular Function

• GO:0003856 3-dehydroquinate synthase activity
• GO:0016838 carbon-oxygen lyase activity, acting on phosphates

Biological Process

• GO:0009073 aromatic amino acid family biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1nvb, PDBe:1nvb, PDBj:1nvb
• PDBsum: 1nvb
• PubMed: 12614613
• UniProt: P07547|ARO1_EMENI Pentafunctional AROM polypeptide (Gene Name=aromA)