Structure of PDB 5u88 Chain B

Receptor sequence
>5u88B (length=208) Species: 562 (Escherichia coli) [Search protein sequence]
MKLAPYILELLTSVNRTNGTADLLVPLLRELAKGRPVSRTTLAGILDWPA
ERVAAVLEQATSTEYDKDGNIIGYGLTLRETSYVFEIDDRRLYAWCALDT
LIFPALIGRTARVSSHCAATGAPVSLTVSPSEIQAVEPAGMAVSLVLPQE
AADVRQSFCCHVHFFASVPTAEDWASKHQGLEGLAIVSVHEAFGLGQEFN
RHLLQTMS
3D structure
PDB5u88 Structural and Biochemical Characterization of Organotin and Organolead Compounds Binding to the Organomercurial Lyase MerB Provide New Insights into Its Mechanism of Carbon-Metal Bond Cleavage.
ChainB
Resolution1.801 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C96 D99 C159
Catalytic site (residue number reindexed from 1) C96 D99 C159
Enzyme Commision number 4.99.1.2: alkylmercury lyase.
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 ZN9 B D99 F158 D99 F158
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0018836 alkylmercury lyase activity
Biological Process
GO:0046689 response to mercury ion

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Molecular Function
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Biological Process
External links
PDB RCSB:5u88, PDBe:5u88, PDBj:5u88
PDBsum5u88
PubMed27989130
UniProtP77072|MERB_ECOLX Alkylmercury lyase (Gene Name=merB)

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