Structure of PDB 1nve Chain B

Receptor sequence

>1nveB (length=383) Species: 162425 (Aspergillus nidulans)

NPTKISILGRESIIADFGLWRNYVAKDLISDCSSTTYVLVTDTNIGSIYT
PSFEEAFRKRAAEITPSPRLLIYNRPPGEVSKSRQTKADIEDWMLSQNPP
CGRDTVVIALGGGVIGDLTGFVASTYMRGVRYVQVPTTLLAMVDSSIGGK
TAIDTPLGKNLIGAIWQPTKIYIDLEFLETLPVREFINGMAEVIKTAAIS
SEEEFTALEENAETILKAVRREVTPGEHRFEGTEEILKARILASARHKAY
VVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELA
RHLGILKGVAVSRIVKCLAAYGLPTSLKDARIRKLTAGKHCSVDQLMFNM
ALKKIVLLSAIGTPYETRASVVANEDIRVVLAP

3D structure

• PDB: 1nve Ligand-induced Conformational Changes and a Mechanism for Domain Closure in Aspergillus nidulans Dehydroquinate Synthase
• Chain: B
• Resolution: 2.58 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	NAD	B	D44 N46 I47 E81 K84 G114 G115 V116 D119 T139 T140 D146 S147 K152 F179 T182 L183 P184 E187	D42 N44 I45 E79 K82 G112 G113 V114 D117 T137 T138 D144 S145 K150 F177 T180 L181 P182 E185

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