Structure of PDB 3t8q Chain B

Receptor sequence
>3t8qB (length=369) Species: 411684 (Hoeflea phototrophica DFL-43) [Search protein sequence]
QSMKIADIETFANEFVCFVKVTTDSGETGWGQVAPYYADITAQVLHRQVA
PYALGKPALDIDYLVDIIPEKEHKFPGSYLRRALGGLDTALWDLRGRLEG
KPVCELIGGTPGTVRAYGSSMKRDITPKDEAARLSRLRDRFGFDAFKFRI
GAECGRGQDEWPGRTEEIVPTIRAAMDDSVALLVDANSCYGPEQAIEVGK
MLEQNGISHYEEPCPYWEYEQTQQVTNALSIDVTGGEQDCELQNWRRMIE
MKAVDIVQPDICYLGGITRTLRVAEMAHKAGLPCTPHAANLSMVTLFTMH
LLRAIPNAGKYLEFSIEGEDYYPWQDDLFVASPYEIVDGKATVTDLPGWG
VEVSPTWLETSAHQISTWQ
3D structure
PDB3t8q Crystal structure of mandelate racemase/muconate lactonizing enzyme family protein from Hoeflea phototrophica
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S118 K145 R147 D157 D183 N185 E209 G234 E235 D237 Q256 D258 H285 A286 A287 K308 E311
Catalytic site (residue number reindexed from 1) S120 K147 R149 D159 D185 N187 E211 G236 E237 D239 Q258 D260 H287 A288 A289 K310 E313
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 B D183 E209 E235 D185 E211 E237
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016836 hydro-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0009063 amino acid catabolic process
GO:0016052 carbohydrate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3t8q, PDBe:3t8q, PDBj:3t8q
PDBsum3t8q
PubMed
UniProtA9D2J3

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