BioLiP

Structure of PDB 1o9b Chain A

Receptor sequence

>1o9bA (length=280) Species: 562 (Escherichia coli) [Search protein sequence]

YELIGLMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSFPGAIEGL
KALKMRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIVNDDGYLRGYNT
DGTGHIRAIKESGFDIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLFNR
RDEFFDKALAFAQRVNENTDCVVTVTDLADQQAFAEALASADILTNGTKV
GMKPLENESLVNDISLLHPGLLVTECVYNPHMTKLLQQAQQAGCKTIDGY
GMLLWQGAEQFTLWTGKDFPLEYVKQVMGF

3D structure

PDB

1o9b Structures of Shikimate Dehydrogenase Aroe and its Paralog Ydib: A Common Structural Framework for Different Activities

Chain

Resolution

2.5 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	A	A132 G133 G134 A135 R156 F160 K205 V206 M208 C232 Y234 M258 L259	A126 G127 G128 A129 R150 F154 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

View graph for
Molecular Function

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Biological Process

PDB	RCSB:1o9b, PDBe:1o9b, PDBj:1o9b
PDBsum	1o9b
PubMed	12637497
UniProt	P0A6D5\|YDIB_ECOLI Quinate/shikimate dehydrogenase (Gene Name=ydiB)