Structure of PDB 4elx Chain C

Receptor sequence
>4elxC (length=242) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
PDEAMLYAPVEWHDCSEGFEDIRYEKSTDGIAKITINRPQVRNAFRPLTV
KEMIQALADARYDDNIGVIILTGAGDKAFCSGGDVHHLNVLDFQRQIRTC
PKPVVAMVAGYSIGGGHVLHMMCDLTIAADNAIFGQTGPKVGSFDGGWGA
SYMARIVGQKKAREIWFLCRQYDAKQALDMGLVNTVVPLADLEKETVRWC
REMLQNSPMALRCLKAALNADCDGQAGLQELAGNATMLFYMT
3D structure
PDB4elx Active site binding and catalytic role of bicarbonate in 1,4-dihydroxy-2-naphthoyl coenzyme A synthases from vitamin K biosynthetic pathways
ChainC
Resolution2.191 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) G86 H105 L109 G133 V136 G156 S161 D163 G164 A250 Y258
Catalytic site (residue number reindexed from 1) G83 H87 L91 G115 V118 G138 S143 D145 G146 A232 Y240
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 CL C G132 Q154 T155 G156 W184 G114 Q136 T137 G138 W166
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4elx, PDBe:4elx, PDBj:4elx
PDBsum4elx
PubMed22606952
UniProtP0ABU0|MENB_ECOLI 1,4-dihydroxy-2-naphthoyl-CoA synthase (Gene Name=menB)

[Back to BioLiP]