Structure of PDB 4b28 Chain A

Receptor sequence
>4b28A (length=437) Species: 375451 (Roseobacter denitrificans OCh 114) [Search protein sequence]
RKIDPSRGATLGDGSPNDMNRVEIGPTQLAFAEWHTARLDLPDLAAMRRF
RHRRLTDHVVARGYAGLLMFDPLNIRYATDSTNMQLWNTHNPFRATLLCA
DGYMVMWDYKNSPFLSEFNPLVREQRAGADLFYFDRGDKVDVAADVFANE
VRILLRDHAPGLRRLAVDKVMLHGLRALQAQGFEIMDGEEVTEKARSVKG
PDEIRAMRCASHACEVAVRKMEDFARSKVGDGVTCENDIWAILHSENVRR
GGEWIETRLLASGPRSNPWFQECGPRVCQRNEIISFDTDLVGAYGICTDI
SRSWWIGDQKPRADMIYAMQHGVEHIRTNMEMLKPGVMIPELSANTHVLD
AKFQKQKYGCLMHGVGLCDEWPLVAYPDHAVAGAYDYPLEPGMTLCVEAL
ISEEGGDFSIKLEDQVLITEDGYENLTKYPFDPALMG
3D structure
PDB4b28 The Structure of Rddddp from Roseobacter Denitrificans Reveals that Dmsp Lyases in the Dddp-Family are Metalloenzymes.
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S23
Catalytic site (residue number reindexed from 1) S15
Enzyme Commision number 4.4.1.3: dimethylpropiothetin dethiomethylase.
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 FE A D295 D297 D307 E421 D287 D289 D299 E413
BS02 FE A D307 H371 E406 E421 D299 H363 E398 E413
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
GO:0047869 dimethylpropiothetin dethiomethylase activity

View graph for
Molecular Function
External links
PDB RCSB:4b28, PDBe:4b28, PDBj:4b28
PDBsum4b28
PubMed25054772
UniProtQ166H0|DDDP_ROSDO Dimethylsulfonioproprionate lyase DddP (Gene Name=dddP)

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