Structure of PDB 1wuf Chain B

Receptor sequence
>1wufB (length=371) Species: 272626 (Listeria innocua Clip11262) [Search protein sequence]
HMYFQKARLIHAELPLLAPFKTSYGELKSKDFYIIELINEEGIHGYGELE
AFPLPDYTEETLSSAILIIKEQLLPLLAQRKIRKPEEIQELFSWIQGNEM
AKAAVELAVWDAFAKMEKRSLAKMIGATKESIKVGVSIGLQQNVETLLQL
VNQYVDQGYERVKLKIAPNKDIQFVEAVRKSFPKLSLMADANSAYNREDF
LLLKELDQYDLEMIEQPFGTKDFVDHAWLQKQLKTRICLDENIRSVKDVE
QAHSIGSCRAINLKLARVGGMSSALKIAEYCALNEILVWCGGMLEAGVGR
AHNIALAARNEFVFPGDISASNRFFAEDIVTPAFELNQGRLKVPTNEGIG
VTLDLKVLKKYTKSTEEILLN
3D structure
PDB1wuf Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family
ChainB
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F2019 A2050 L2053 S2136 K2162 K2164 D2189 N2191 E2214 D2239 E2240 N2241 K2263 L2286 G2290 G2291 M2292 D2316 I2317
Catalytic site (residue number reindexed from 1) F20 A51 L54 S137 K163 K165 D190 N192 E215 D240 E241 N242 K264 L287 G291 G292 M293 D317 I318
Enzyme Commision number 4.2.1.113: o-succinylbenzoate synthase.
5.1.1.-
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 E2214 D2239 E215 D240
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0016853 isomerase activity
GO:0043748 O-succinylbenzoate synthase activity
GO:0046872 metal ion binding
Biological Process
GO:0009234 menaquinone biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1wuf, PDBe:1wuf, PDBj:1wuf
PDBsum1wuf
PubMed24872444
UniProtQ927X3|MENC_LISIN o-succinylbenzoate synthase (Gene Name=menC)

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