Structure of PDB 3zok Chain D

Receptor sequence
>3zokD (length=365) Species: 3625 (Actinidia chinensis) [Search protein sequence]
PTIVDVDLGDRSYPIYIGSGLLDQPDLLQRHVHGKRVLVVTNSTVAPIYL
DKVVGALTNENPNVSVESVILPDGEKYKNMDTLMKVFDKAIESRLDRRCT
FVALGGGVIGDMCGYAAASFLRGVNFIQIPTTVMAQVDSSVGGKTGINHR
LGKNLIGAFYQPQCVLIDTDTLNTLPDRELASGLAEVVKYGLIRDANFFE
WQEKNMPALMARDPSALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHT
FGHAIETGFGYGQWLHGEAVAAGMVMAVDMSYRLGWIDESIVNRAHNILQ
QAKLPTAPPETMTVEMFKSVMAVDKKVADGLLRLILLKGPLGNCVFTGDY
DRKALDETLHAFCKS
3D structure
PDB3zok Biochemical and structural characterisation of dehydroquinate synthase from the New Zealand kiwifruit Actinidia chinensis.
ChainD
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R134 K156 E198 K240 E250 R254 N258 H261 H265 H278
Catalytic site (residue number reindexed from 1) R122 K144 E186 K228 E238 R242 N246 H249 H253 H266
Enzyme Commision number 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 NAD D N54 V57 D85 E87 K90 G118 G119 V120 D123 T143 T144 M146 D150 S151 K165 T186 L187 E191 H278 N42 V45 D73 E75 K78 G106 G107 V108 D111 T131 T132 M134 D138 S139 K153 T174 L175 E179 H266
BS02 GLY D N185 T186 L187 N173 T174 L175
BS03 GLY D K350 D361 K338 D349
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:3zok, PDBe:3zok, PDBj:3zok
PDBsum3zok
PubMed23916589
UniProtU3KRF2|DHQS_ACTCC 3-dehydroquinate synthase, chloroplastic (Gene Name=DHQS)

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