Structure of PDB 1o9b Chain B

Receptor sequence
>1o9bB (length=280) Species: 562 (Escherichia coli) [Search protein sequence]
YELIGLMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSFPGAIEGL
KALKMRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIVNDDGYLRGYNT
DGTGHIRAIKESGFDIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLFNR
RDEFFDKALAFAQRVNENTDCVVTVTDLADQQAFAEALASADILTNGTKV
GMKPLENESLVNDISLLHPGLLVTECVYNPHMTKLLQQAQQAGCKTIDGY
GMLLWQGAEQFTLWTGKDFPLEYVKQVMGF
3D structure
PDB1o9b Structures of Shikimate Dehydrogenase Aroe and its Paralog Ydib: A Common Structural Framework for Different Activities
ChainB
Resolution2.5 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 NAI B A132 G133 G134 A135 N155 R156 D158 F160 T204 K205 V206 M208 C232 Y234 M258 L259 A126 G127 G128 A129 N149 R150 D152 F154 T198 K199 V200 M202 C226 Y228 M252 L253
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:1o9b, PDBe:1o9b, PDBj:1o9b
PDBsum1o9b
PubMed12637497
UniProtP0A6D5|YDIB_ECOLI Quinate/shikimate dehydrogenase (Gene Name=ydiB)

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