Structure of PDB 1nve Chain C

Receptor sequence

>1nveC (length=377) Species: 162425 (Aspergillus nidulans)

PTKISILGRESIIADFGLWRNYVAKDLISDCSSTTYVLVTDTNIGSIYTP
SFEEAFRKRAAEITPSPRLLIYNRPPGEVSKSRQTKADIEDWMLSQNPPC
GRDTVVIALGGGVIGDLTGFVASTYMRGVRYVQVPTTLLAMVDSSIGGKT
AIDTPLGKNLIGAIWQPTKIYIDLEFLETLPVREFINGMAEVIKTAAISS
EEEFTALEENAETILKAVRREVTPGEHRFEGTEEILKARILASARHKAYV
VSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELAR
HLGILKGVAVSRIVKCLAAYGLPTSLKDARIRKLTAGKHCSVDQLMFNMV
LLSAIGTPYETRASVVANEDIRVVLAP

3D structure

• PDB: 1nve Ligand-induced Conformational Changes and a Mechanism for Domain Closure in Aspergillus nidulans Dehydroquinate Synthase
• Chain: C
• 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): R127 K149 E191 K247 E257 R261 N265 H268 H272 H284
• 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	C	E194 H271 H287	E191 H268 H284
BS02	NAD	C	D44 N46 I47 E81 K84 G114 G115 V116 D119 T139 T140 L142 D146 S147 K152 F179 T182 L183 E187	D41 N43 I44 E78 K81 G111 G112 V113 D116 T136 T137 L139 D143 S144 K149 F176 T179 L180 E184

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)