Structure of PDB 2x7j Chain C Binding Site BS02

Receptor Information
>2x7j Chain C (length=577) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TVNPITHYIGSFIDEFALSGITDAVVCPGSRSTPLAVLCAAHPDISVHVQ
IDERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAHYSRVPIIV
LTADRPHELREVGAPQAINQHFLFGNFVKFFTDSALPEESPQMLRYIRTL
ASRAAGEAQKRPMGPVHVNVPLREPLMPDLSDEPFGRMRTGRHVSVKTGT
QSVDRESLSDVAEMLAEAEKGMIVCGELHSDADKENIIALSKALQYPILA
DPLSNLRNGVHDKSTVIDAYDSFLKDDELKRKLRPDVVIRFGPMPVSKPV
FLWLKDDPTIQQIVIDEDGGWRDPTQASAHMIHCNASVFAEEIMAGLTAA
TRSSEWLEKWQFVNGRFREHLQTISSEDVSFEGNLYRILQHLVPENSSLF
VGNSMPIRDVDTFFEKQDRPFRIYSNRGANGIDGVVSSAMGVCEGTKAPV
TLVIGDLSFYHDLNGLLAAKKLGIPLTVILVNNDGGGIFSFLPQASEKTH
FEDLFGTPTGLDFKHAAALYGGTYSCPASWDEFKTAYAPQADKPGLHLIE
IKTDRQSRVQLHRDMLNEAVREVKKQW
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain2x7j Chain C Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2x7j Structure and Reactivity of Bacillus Subtilis Mend Catalyzing the First Committed Step in Menaquinone Biosynthesis.
Resolution2.35 Å
Binding residue
(original residue number in PDB)		D457 N484 G486
Binding residue
(residue number reindexed from 1)		D456 N483 G485
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) C28 E54
Catalytic site (residue number reindexed from 1) C27 E53
Enzyme Commision number 2.2.1.9: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016740 transferase activity
GO:0030145 manganese ion binding
GO:0030976 thiamine pyrophosphate binding
GO:0046872 metal ion binding
GO:0070204 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity
Biological Process
GO:0009234 menaquinone biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2x7j, PDBe:2x7j, PDBj:2x7j
PDBsum2x7j
PubMed20600129
UniProtP23970|MEND_BACSU 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (Gene Name=menD)

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