Structure of PDB 4i42 Chain L

Receptor sequence
>4i42L (length=285) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MIYPDEAMLYAPVEWHDCSEGFEDIRYEKSTDGIAKITINRPQVRNAFRP
LTVKEMIQALADARYDDNIGVIILTGAGDKAFCSGGDQKVRGDYGGYKDD
SGVHHLNVLDFQRQIRTCPKPVVAMVAGYSIGGGHVLHMMCDLTIAADNA
IFGQTGPKVGSFDGGWGASYMARIVGQKKAREIWFLCRQYDAKQALDMGL
VNTVVPLADLEKETVRWCREMLQNSPMALRCLKAALNADCDGQAGLQELA
GNATMLFYMTEEGQEGRNAFNQKRQPDFSKFKRNP
3D structure
PDB4i42 Structural basis of the induced-fit mechanism of 1,4-dihydroxy-2-naphthoyl coenzyme A synthase from the crotonase fold superfamily
ChainL
Resolution1.848 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 R91 Y97 H105 L109 G133 V136 G156 S161 D163 G164 A250 Y258
Catalytic site (residue number reindexed from 1) G86 R91 Y97 H105 L109 G133 V136 G156 S161 D163 G164 A250 Y258
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 1HA L T254 F270 K273 T254 F270 K273
BS02 1HA L V44 R45 A47 S84 G85 G86 D87 Q88 Y97 V108 L109 Y129 G133 T155 S161 V44 R45 A47 S84 G85 G86 D87 Q88 Y97 V108 L109 Y129 G133 T155 S161
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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Cellular Component
External links
PDB RCSB:4i42, PDBe:4i42, PDBj:4i42
PDBsum4i42
PubMed23658663
UniProtP0ABU0|MENB_ECOLI 1,4-dihydroxy-2-naphthoyl-CoA synthase (Gene Name=menB)

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