Structure of PDB 1nvb Chain A

Receptor sequence
>1nvbA (length=390) Species: 162425 (Aspergillus nidulans) [Search protein sequence]
NPTKISILGRESIIADFGLWRNYVAKDLISDCSSTTYVLVTDTNIGSIYT
PSFEEAFRKRAAEITPSPRLLIYNRPPGEVSKSRQTKADIEDWMLSQNPP
CGRDTVVIALGGGVIGDLTGFVASTYMRGVRYVQVPTTLLAMVDSSIGGK
TAIDTPLGKNLIGAIWQPTKIYIDLEFLETLPVREFINGMAEVIKTAAIS
SEEEFTALEENAETILKAVRREVTPGEHRFEGTEEILKARILASARHKAY
VVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELA
RHLGILKGVAVSRIVKCLAAYGLPTSLKDARIRKLTAGKHCSVDQLMFNM
ALDKKNDGPKKKIVLLSAIGTPYETRASVVANEDIRVVLA
3D structure
PDB1nvb Ligand-induced Conformational Changes and a Mechanism for Domain Closure in Aspergillus nidulans Dehydroquinate Synthase
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1nvb, PDBe:1nvb, PDBj:1nvb
PDBsum1nvb
PubMed12614613
UniProtP07547|ARO1_EMENI Pentafunctional AROM polypeptide (Gene Name=aromA)

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