Structure of PDB 1sg6 Chain A

Receptor sequence

>1sg6A (length=377) Species: 162425 (Aspergillus nidulans)

PTKISILGRESIIADFGLWRNYVAKDLISDCSSTTYVLVTDTNIGSIYTP
SFEEAFRKRAAEITPSPRLLIYNRPPGEVSKSRQTKADIEDWMLSQNPPC
GRDTVVIALGGGVIGDLTGFVASTYMRGVRYVQVPTTLLAMVDSSIGGKT
AIDTPLGKNLIGAIWQPTKIYIDLEFLETLPVREFINGMAEVIKTAAISS
EEEFTALEENAETILKAVRREVTPGEHRFEGTEEILKARILASARHKAYV
VSAGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGIL
KGVAVSRIVKCLAAYGLPTSLKDARIRKLTAGKHCSVDQLMFNMALDKKI
VLLSAIGTPYETRASVVANEDIRVVLA

3D structure

• PDB: 1sg6 Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 A resolution from crystals grown following enzyme turnover.
• Chain: A
• Resolution: 1.7 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 R256 N260 H263 H267 H279
• 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	A	E194 H271 H287	E191 H263 H279
BS02	NAD	A	D44 N46 I47 K84 G114 G115 V116 D119 T139 T140 S147 F179 T182 L183 E187	D41 N43 I44 K81 G111 G112 V113 D116 T136 T137 S144 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:1sg6, PDBe:1sg6, PDBj:1sg6
• PDBsum: 1sg6
• PubMed: 15103156
• UniProt: P07547|ARO1_EMENI Pentafunctional AROM polypeptide (Gene Name=aromA)