Structure of PDB 1nva Chain B

Receptor sequence

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

PTKISILGRESIIADFGLWRNYVAKDLISDCSSTTYVLVTDTNIGSIYTP
SFEEAFRKRAAEITPSPRLLIYNRPPGEVSKSRQTKADIEDWMLSQNPPC
GRDTVVIALGGGVIGDLTGFVASTYMRGVRYVQVPTTLLAMVDSSIGGKT
AIDTPLGKNLIGAIWQPTKIYIDLEFLETLPVREFINGMAEVIKTAAISS
EEEFTALEENAETILKAVRREVTPGEHRFEGTEEILKARILASARHKAYV
VSADGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLG
ILKGVAVSRIVKCLAAYGLPTSLKDARIRKLTAGKHCSVDQLMFNMALDK
GPKKKIVLLSAIGTPYETRASVVANEDIRVVLA

3D structure

• PDB: 1nva Ligand-induced Conformational Changes and a Mechanism for Domain Closure in Aspergillus nidulans Dehydroquinate Synthase
• Chain: B
• Resolution: 2.62 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R130 K152 E194 K250 R264 N268 H271 H275 H287
• Catalytic site (residue number reindexed from 1): R127 K149 E191 K247 R258 N262 H265 H269 H281
• 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	E191 H265 H281
BS02	ADP	B	D44 N46 I47 G114 G115 V116 T139 T140 F179 T182 L183 E187	D41 N43 I44 G111 G112 V113 T136 T137 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:1nva, PDBe:1nva, PDBj:1nva
• PDBsum: 1nva
• PubMed: 12614613
• UniProt: P07547|ARO1_EMENI Pentafunctional AROM polypeptide (Gene Name=aromA)