Structure of PDB 1r9d Chain B

Receptor sequence
>1r9dB (length=786) Species: 1492 (Clostridium butyricum) [Search protein sequence]
ISKGFSTQTERINILKAQILNAKPCVESERAILITESFKQTEGQPAILRR
ALALKHILENIPITIRDQELIVGSLTKEPRSSQVFPEFSNKWLQDELDRL
NKRTGDAFQISEESKEKLKDVFEYWNGKTTSELATSYMTEETREAVNCDV
FTVGNYYYNGVGHVSVDYGKVLRVGFNGIINEAKEQLEKNRSIDPDFIKK
EKFLNSVIISCEAAITYVNRYAKKAKEIADNTSDAKRKAELNEIAKICSK
VSGEGAKSFYEACQLFWFIHAIINIESNGHSISPARFDQYMYPYYENDKN
ITDKFAQELIDCIWIKLNDINKVRDEISTKHFGGYPMYQNLIVGGQNSEG
KDATNKVSYMALEAAVHVKLPQPSLSVRIWNKTPDEFLLRAAELTREGLG
LPAYYNDEVIIPALVSRGLTLEDARDYGIIGCVEPQKPGKTEGWHDSAFF
NLARIVELTINSGFDKNKQIGPKTQNFEEMKSFDEFMKAYKAQMEYFVKH
MCCADNCIDIAHAERAPLPFLSSMVDNCIGKGKSLQDGGAEYNFSGPQGV
GVANIGDSLVAVKKIVFDENKITPSELKKTLNNDFKNSEEIQALLKNAPK
FGNDIDEVDNLAREGALVYCREVNKYTNPRGGNFQPGLYPSSINVYFGSL
TGATPDGRKSGQPLADGVSPSRGCDVSGPTAACNSVSKLDHFIASNGTLF
NQKFHPSALKGDNGLMNLSSLIRSYFDQKGFHVQFNVIDKKILLAAQKNP
EKYQDLIVRVAGYSAQFISLDKSIQNDIIARTEHVM
3D structure
PDB1r9d Insight into the mechanism of the B12-independent glycerol dehydratase from Clostridium butyricum: preliminary biochemical and structural characterization.
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y339 G432 C433 G763
Catalytic site (residue number reindexed from 1) Y338 G431 C432 G762
Enzyme Commision number ?
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 GOL B H164 H281 S282 Y339 C433 E435 D447 Y640 H163 H280 S281 Y338 C432 E434 D446 Y639
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:1r9d, PDBe:1r9d, PDBj:1r9d
PDBsum1r9d
PubMed15096031
UniProtQ8GEZ8

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