Structure of PDB 2x7j Chain D

Receptor sequence
>2x7jD (length=579) Species: 1423 (Bacillus subtilis) [Search protein sequence]
TVNPITHYIGSFIDEFALSGITDAVVCPGSRSTPLAVLCAAHPDISVHVQ
IDERSAGFFALGLAKAKQRPVLLICTSGTAAANFYPAVVEAHYSRVPIIV
LTADRPHELREVGAPQAINQHFLFGNFVKFFTDSALPEESPQMLRYIRTL
ASRAAGEAQKRPMGPVHVNVPLREPLMPDLSDEPFGRMRTGRHVSVKTGT
QSVDRESLSDVAEMLAEAEKGMIVCGELHSDADKENIIALSKALQYPILA
DPLSNLRNGVHDKSTVIDAYDSFLKDDELKRKLRPDVVIRFGPMPVSKPV
FLWLKDDPTIQQIVIDEDGGWRDPTQASAHMIHCNASVFAEEIMAGLTAA
TRSSEWLEKWQFVNGRFREHLQTISSEDVSFEGNLYRILQHLVPENSSLF
VGNSMPIRDVDTFFEKQDRPFRIYSNRGANGIDGVVSSAMGVCEGTKAPV
TLVIGDLSFYHDLNGLLAAKKLGIPLTVILVNNDGGGIFSFLPQASEKTH
FEDLFGTPTGLDFKHAAALYGGTYSCPASWDEFKTAYAPQADKPGLHLIE
IKTDRQSRVQLHRDMLNEAVREVKKQWEL
3D structure
PDB2x7j Structure and Reactivity of Bacillus Subtilis Mend Catalyzing the First Committed Step in Menaquinone Biosynthesis.
ChainD
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 TPP D P29 E54 P28 E53
BS02 TPP D S405 M406 I433 D434 G456 D457 L458 S459 N484 G486 G487 G488 I489 F490 S404 M405 I432 D433 G455 D456 L457 S458 N483 G485 G486 G487 I488 F489
BS03 MN D D457 N484 G486 D456 N483 G485
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

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Molecular Function
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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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