Structure of PDB 1vi2 Chain A

Receptor sequence
>1vi2A (length=284) Species: 562 (Escherichia coli) [Search protein sequence]
AKYELIGLMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSFPGAIE
GLKALKMRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIVNDDGYLRGY
NTDGTGHIRAIKESGFDIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLF
NRRDEFFDKALAFAQRVNENTDCVVTVTDLADQQAFAEALASADILTNGT
KVGMKPLENESLVNDISLLHPGLLVTECVYNPHMTKLLQQAQQAGCKTID
GYGMLLWQGAEQFTLWTGKDFPLEYVKQVMGFGA
3D structure
PDB1vi2 Structural analysis of a set of proteins resulting from a bacterial genomics project
ChainA
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.282: quinate/shikimate dehydrogenase [NAD(P)(+)].
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 A G131 G133 G134 A135 N155 R156 D158 F160 T204 K205 V206 M208 C232 M258 L259 G127 G129 G130 A131 N151 R152 D154 F156 T200 K201 V202 M204 C228 M254 L255
Gene Ontology
Molecular Function
GO:0004764 shikimate 3-dehydrogenase (NADP+) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0030266 quinate 3-dehydrogenase (NAD+) activity
GO:0042803 protein homodimerization activity
GO:0052733 quinate 3-dehydrogenase (NADP+) activity
GO:0052734 shikimate 3-dehydrogenase (NAD+) activity
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009073 aromatic amino acid family biosynthetic process
GO:0009423 chorismate biosynthetic process
GO:0019632 shikimate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1vi2, PDBe:1vi2, PDBj:1vi2
PDBsum1vi2
PubMed16021622
UniProtP0A6D5|YDIB_ECOLI Quinate/shikimate dehydrogenase (Gene Name=ydiB)

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