Structure of PDB 1wuf Chain B Binding Site BS01

Receptor Information
>1wuf Chain B (length=371) Species: 272626 (Listeria innocua Clip11262) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMYFQKARLIHAELPLLAPFKTSYGELKSKDFYIIELINEEGIHGYGELE
AFPLPDYTEETLSSAILIIKEQLLPLLAQRKIRKPEEIQELFSWIQGNEM
AKAAVELAVWDAFAKMEKRSLAKMIGATKESIKVGVSIGLQQNVETLLQL
VNQYVDQGYERVKLKIAPNKDIQFVEAVRKSFPKLSLMADANSAYNREDF
LLLKELDQYDLEMIEQPFGTKDFVDHAWLQKQLKTRICLDENIRSVKDVE
QAHSIGSCRAINLKLARVGGMSSALKIAEYCALNEILVWCGGMLEAGVGR
AHNIALAARNEFVFPGDISASNRFFAEDIVTPAFELNQGRLKVPTNEGIG
VTLDLKVLKKYTKSTEEILLN
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1wuf Chain B Residue 5002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1wuf Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family
Resolution2.9 Å
Binding residue
(original residue number in PDB)		E2214 D2239
Binding residue
(residue number reindexed from 1)		E215 D240
Annotation score1
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.-
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

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

[Back to BioLiP]