Structure of PDB 3sqs Chain A

Receptor sequence

>3sqsA (length=386) Species: 398580 (Dinoroseobacter shibae DFL 12 = DSM 16493) [Search protein sequence]

MTKIKSVRTRVWNWTGPTVPPQGNFCTNASDALWIASFRFHQWLTCEVET
EDGTIGIGNAALAPNVVKQAIDEWYAPLVIGEDPFDYAYLWEKMYRRTHA
WGRKGIGMTAISAIDIAIWDLMGKLVGKPVFKLLGGRTKEKIPVYYSKLY
ADSIPAMQAEAEEAQKHGYQGYKTRFGYGPKDGPAGMRENLKRVEALREV
LGYDVDLMLECYMGWNLDYTKRMLPKLERFEPRWLEEPVIADDVAGYAEL
NAMGIVPISGGEHEFSVMGCAELINRKAVSVLQYDTNRVGGITAAQKINA
IAEAAQIIVIPHAGQMHNYHLTMANMNCPISEYFPVFDVEVGNELFYYIF
DGDPEAVDGYLQLDDDTPGLGITISDAHLKHFEITE

3D structure

PDB

3sqs Crystal Structure of a putative mandelate racemase/muconate lactonizing protein from Dinoroseobacter shibae DFL 12

Chain

Resolution

1.9 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	L89 N92 S174 K200 R202 G204 G206 K208 A212 E237 Y239 E263 G288 E289 H290 Q310 D312 I334 H339 G341 E359 F364
Catalytic site (residue number reindexed from 1)	L62 N65 S147 K173 R175 G177 G179 K181 A185 E210 Y212 E236 G261 E262 H263 Q283 D285 I307 H312 G314 E332 F337
Enzyme Commision number	?

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	MG	A	E237 E263 E289	E210 E236 E262
BS02	MG	A	Y374 F377 D378	Y347 F350 D351

Gene Ontology

	Molecular Function
GO:0000287	magnesium ion binding
GO:0016836	hydro-lyase activity
GO:0046872	metal ion binding
GO:0050032	L-rhamnonate dehydratase activity

	Biological Process
GO:0016052	carbohydrate catabolic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:3sqs, PDBe:3sqs, PDBj:3sqs
PDBsum	3sqs
PubMed
UniProt	A8LS88

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