Structure of PDB 4elw Chain E

Receptor sequence
>4elwE (length=260) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
DEAMLYAPVEWHDCSEGFEDIRYEKSTDGIAKITINRPQVRNAFRPLTVK
EMIQALADARYDDNIGVIILTGAGDKAFCSGGDVHHLNVLDFQRQIRTCP
KPVVAMVAGYSIGGGHVLHMMCDLTIAADNAIFGQTGPKVGSFDGGWGAS
YMARIVGQKKAREIWFLCRQYDAKQALDMGLVNTVVPLADLEKETVRWCR
EMLQNSPMALRCLKAALNADCDGQAGLQELAGNATMLFYMTEEGQEGRNA
PDFSKFKRNP
3D structure
PDB4elw Active site binding and catalytic role of bicarbonate in 1,4-dihydroxy-2-naphthoyl coenzyme A synthases from vitamin K biosynthetic pathways
ChainE
Resolution2.551 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G86 L109 G133 V136 G156 S161 D163 G164 A250 Y258
Catalytic site (residue number reindexed from 1) G82 L90 G114 V117 G137 S142 D144 G145 A231 Y239
Enzyme Commision number 4.1.3.36: 1,4-dihydroxy-2-naphthoyl-CoA 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 NO3 E G132 Q154 G156 F162 W184 G113 Q135 G137 F143 W165
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0008935 1,4-dihydroxy-2-naphthoyl-CoA synthase activity
GO:0016829 lyase activity
GO:0071890 bicarbonate binding
Biological Process
GO:0009234 menaquinone biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4elw, PDBe:4elw, PDBj:4elw
PDBsum4elw
PubMed22606952
UniProtP0ABU0|MENB_ECOLI 1,4-dihydroxy-2-naphthoyl-CoA synthase (Gene Name=menB)

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